BRENDA - Enzyme Database show
show all sequences of 3.4.21.41

A molecular dynamics study of C1r and C1s dimers: implications for the structure of the C1 complex

Beveridge, A.J.; Wallis, R.; Samani, N.J.; Proteins 80, 1987-1997 (2012)

Data extracted from this reference:

Crystallization (Commentary)
Crystallization
Organism
crystal structure analysis, PDB IDs 1APQ
Homo sapiens
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Homo sapiens
P00736
-
-
Subunits
Subunits
Commentary
Organism
More
each C1r monomer consists of six domains, CUB1-EGF-CUB2-CCP1-CCP2-SP, i.e. an N-terminal CUB module, an EGF-like module, a second CUB module, two complement control modules CCP, and a serine protease domain SP. The three domains that constitute the catalytic fragment of C1r (CCP1-CCP2-SP) readily form head-to-tail dimers. The CUB1-EGF-CUB2 fragments of C1r also dimerize
Homo sapiens
Crystallization (Commentary) (protein specific)
Crystallization
Organism
crystal structure analysis, PDB IDs 1APQ
Homo sapiens
Subunits (protein specific)
Subunits
Commentary
Organism
More
each C1r monomer consists of six domains, CUB1-EGF-CUB2-CCP1-CCP2-SP, i.e. an N-terminal CUB module, an EGF-like module, a second CUB module, two complement control modules CCP, and a serine protease domain SP. The three domains that constitute the catalytic fragment of C1r (CCP1-CCP2-SP) readily form head-to-tail dimers. The CUB1-EGF-CUB2 fragments of C1r also dimerize
Homo sapiens
General Information
General Information
Commentary
Organism
metabolism
complement is an important part of the immune system. It is initiated through three different pathways known as the classical, lectin, and alternative pathway. The multimolecular C1 complex of the classical pathway consists of a subcomponent, C1q, which binds to a tetramer comprising two C1r and two C1s proteases, EC 3.4.21.41 and EC 3.4.21.42, respectively
Homo sapiens
additional information
the C1s/C1r/C1r/C1s tetramer forms a complex with C1q by interacting with the stems. C1r is a homologous multidomain protease containing an N-terminal CUB module, an EGF-like module, a second CUB module, two complement control modules CCP, and a serine protease domain SP. The three domains that constitute the catalytic fragment of C1r (CCP1-CCP2-SP) readily form head-to-tail dimers. The CUB1-EGF-CUB2 fragments of C1r also dimerize. Interaction analysis and structure-function relationship, formation of the C1 complex, molecular dynamics simulations and thermodynamics, detailed overview
Homo sapiens
physiological function
C1r is a zymogen, activation of C1 occurs when the C1q subcomponent binds to a pathogen via its globular heads resulting in autolytic activation of C1r followed, in turn, by C1r-mediated activation of C1s
Homo sapiens
General Information (protein specific)
General Information
Commentary
Organism
metabolism
complement is an important part of the immune system. It is initiated through three different pathways known as the classical, lectin, and alternative pathway. The multimolecular C1 complex of the classical pathway consists of a subcomponent, C1q, which binds to a tetramer comprising two C1r and two C1s proteases, EC 3.4.21.41 and EC 3.4.21.42, respectively
Homo sapiens
additional information
the C1s/C1r/C1r/C1s tetramer forms a complex with C1q by interacting with the stems. C1r is a homologous multidomain protease containing an N-terminal CUB module, an EGF-like module, a second CUB module, two complement control modules CCP, and a serine protease domain SP. The three domains that constitute the catalytic fragment of C1r (CCP1-CCP2-SP) readily form head-to-tail dimers. The CUB1-EGF-CUB2 fragments of C1r also dimerize. Interaction analysis and structure-function relationship, formation of the C1 complex, molecular dynamics simulations and thermodynamics, detailed overview
Homo sapiens
physiological function
C1r is a zymogen, activation of C1 occurs when the C1q subcomponent binds to a pathogen via its globular heads resulting in autolytic activation of C1r followed, in turn, by C1r-mediated activation of C1s
Homo sapiens
Other publictions for EC 3.4.21.41
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [C]
Temperature Range [C]
Temperature Stability [C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [C] (protein specific)
Temperature Range [C] (protein specific)
Temperature Stability [C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
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Structural basis of the C1q/C1 ...
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110
13916-13920
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Expression of recombinant huma ...
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Proc. Natl. Acad. Sci. USA
110
8650-8655
2013
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732889
Beveridge
A molecular dynamics study of ...
Homo sapiens
Proteins
80
1987-1997
2012
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Lang
Intermodule cooperativity in t ...
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FEBS J.
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Homo sapiens
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717786
Major
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Homo sapiens
J. Biol. Chem.
285
11863-11869
2010
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Homo sapiens
J. Biol. Chem.
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718116
Valck
Molecular mechanisms involved ...
Homo sapiens
Mol. Immunol.
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1516-1521
2010
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718117
Kaplan
The plasma bradykinin-forming ...
Homo sapiens
Mol. Immunol.
47
2161-2169
2010
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683195
Duncan
The initiating proteases of th ...
Homo sapiens
Biochimie
90
387-395
2008
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683889
Kardos
Revisiting the mechanism of th ...
Homo sapiens
Mol. Immunol.
45
1752-1760
2008
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696932
Gaultier
Regulation of tumor necrosis f ...
Mus musculus
Blood
111
5316-5325
2008
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697529
Goesswein
Mutational spectrum of the C1I ...
Homo sapiens
Cytogenet. Genome Res.
121
181-188
2008
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698805
Geach
Molecular determinants of Xoll ...
Xenopus laevis
J. Biol. Chem.
283
27057-27063
2008
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700245
Davis
Biological activities of C1 in ...
Homo sapiens
Mol. Immunol.
45
4057-4063
2008
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683530
Biro
Studies on the interactions be ...
Homo sapiens
Immunology
121
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2007
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650989
Budayova-Spano
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Homo sapiens
EMBO J.
21
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2002
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653898
Budayova-Spano
Monomeric structures of the zy ...
Homo sapiens
Structure
10
1509-1519
2002
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652176
Lacroix
Assembly and enzymatic propert ...
Homo sapiens
J. Biol. Chem.
276
36233-36240
2001
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652680
Kardos
The role of the individual dom ...
Homo sapiens
J. Immunol.
167
5202-5208
2001
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81405
Dobo
One active C1r subunit is suff ...
Homo sapiens
J. Immunol.
162
1108-1112
1999
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81391
Gal
Structure and function of the ...
Homo sapiens
Immunobiology
199
317-326
1998
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81388
Thielens
Activation of human complement ...
Homo sapiens
Biochem. J.
301
509-516
1994
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1
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-
81390
Illy
Chemical characterization and ...
Homo sapiens
J. Protein Chem.
12
771-781
1993
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1
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1
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1
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1
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1
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1
1
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81400
Katz
Regulation of synthesis of com ...
Homo sapiens
Clin. Immunol. Immunopathol.
67
117-123
1993
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1
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1
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1
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1
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1
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1
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81401
Zavodszky
Protein engineering studies on ...
Homo sapiens
Behring Inst. Mitt.
93
103-114
1993
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1
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1
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1
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1
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81402
Gulati
Regulation of the synthesis of ...
Homo sapiens
Behring Inst. Mitt.
93
196-203
1993
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1
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5
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5
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81403
Arlaud
Human complement serine protea ...
Homo sapiens
Methods Enzymol.
223
61-82
1993
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1
6
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1
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2
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1
1
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1
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4
1
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1
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1
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1
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6
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1
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1
1
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1
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4
1
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1
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1
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81404
Kam
Substituted isocoumarins as in ...
Homo sapiens
J. Immunol.
149
163-168
1992
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3
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1
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3
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81399
Thielens
Ca2+ binding properties and Ca ...
Homo sapiens
J. Biol. Chem.
265
14469-14475
1990
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1
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1
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1
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81386
Busby
Calcium-sensitive thermal tran ...
Homo sapiens
Biochemistry
26
5564-5571
1987
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2
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1
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1
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1
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1
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81387
Journet
Cloning and sequencing of full ...
Homo sapiens
Biochem. J.
240
783-787
1986
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1
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1
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1
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81397
Reboul
Characteristics of complement ...
Homo sapiens
Biochem. J.
233
559-564
1986
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1
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1
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81389
Loos
-
C1rbar-esterase ...
Homo sapiens
Methods Enzym. Anal. , 3rd Ed. (Bergmeyer, H. U. , ed. )
5
514-527
1984
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3
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3
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3
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81396
Nilsson
Kinetics of the reaction betwe ...
Homo sapiens
Eur. J. Biochem.
129
663-667
1983
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1
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81395
Sim
The human complement system se ...
Homo sapiens
Methods Enzymol.
80
26-42
1981
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5
1
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1
1
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2
1
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4
2
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1
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5
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1
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1
1
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2
1
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4
2
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1
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81394
Sim
Kinetics of reaction of human ...
Homo sapiens
Biochim. Biophys. Acta
612
433-449
1980
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81398
Arlaud
Purified proenzyme C1r. Some c ...
Homo sapiens
Biochim. Biophys. Acta
616
116-129
1980
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1
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1
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1
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1
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1
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81392
Andrews
The enzymatic nature of human ...
Homo sapiens
J. Immunol.
123
1403-1408
1979
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3
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2
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1
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5
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3
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81393
Sim
The structure and enzymic acti ...
Homo sapiens
Biochem. J.
163
219-227
1977
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1
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2
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1
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1
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1
1
1
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