Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 3.4.21.42 extracted from

  • Venkatraman Girija, U.; Gingras, A.R.; Marshall, J.E.; Panchal, R.; Sheikh, M.A.; Gal, P.; Schwaeble, W.J.; Mitchell, D.A.; Moody, P.C.; Wallis, R.
    Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation (2013), Proc. Natl. Acad. Sci. USA, 110, 13916-13920.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 3.4.21.42

Cloned(Commentary)

Cloned (Comment) Organism
expression of the CUB1-EGF-CUB2 region of enzyme C1s in CHO cells Homo sapiens

Crystallization (Commentary)

Crystallization (Comment) Organism
in the absence of collagen peptide, C1s crystallizes to form a tetramer, similar to the native C1r-C1s-C1r-C1s complex. The tetramer is a flat ring with an outer diameter of about 120 A. The structure is assembled from two X-shaped dimers linked via a connecting interface at the center, structure overview Homo sapiens

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ recombinant CUB1-EGF-CUB2 region of enzyme C1s , dependent on, required for substrate binding. The CUB1-EGF-CUB2 domains of C1s are arranged linearly with three Ca2+: one in each CUB domain and one within the EGF-like domain, near the CUB1-EGF junction Homo sapiens

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
complement C1q zymogen + H2O Homo sapiens C1s-C1q Collagen interface, the three collagen-like peptides form a right-handed helix with a characteristic one residue stagger between adjacent strands, overview ?
-
 ?
complement C4 + H2O Homo sapiens
-
 ?
-
 ?
complement C4b-bound C2 + H2O Homo sapiens
-
 ?
-
 ?

Organism

Organism UniProt Comment Textmining
Homo sapiens P09871
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
complement C1q zymogen + H2O C1s-C1q Collagen interface, the three collagen-like peptides form a right-handed helix with a characteristic one residue stagger between adjacent strands, overview Homo sapiens ?
-
 ?
complement C4 + H2O
-
 Homo sapiens ?
-
 ?
complement C4b-bound C2 + H2O
-
 Homo sapiens ?
-
 ?
additional information the enzyme recognizes the a short collagen-like peptide containing the sequence Hyp-Gly-Lys-Leu-Gly-Pro Homo sapiens ?
-
 ?

Subunits

Subunits Comment Organism
dimer recombinant CUB1-EGF-CUB2 region of enzyme C1s, monomers associate to form an X-shaped dimer through lateral association of the CUB1 and EGF-like domains about the crystallographic symmetry axis. The interface features a number of hydrophobic side chains Homo sapiens
tetramer in the absence of collagen peptide, C1s crystallizes to form a tetramer, similar to the native C1r-C1s-C1r-C1s complex. The tetramer is a flat ring with an outer diameter of about 120 A Homo sapiens

Synonyms

Synonyms Comment Organism
protease C1s
-
 Homo sapiens

General Information

General Information Comment Organism
additional information the large multicomponent assembly C1 complex is composed of a recognition subcomponent, C1q (460 kDa), and two serine protease subcomponents, C1r (90 kDa) and C1s (80 kDa) in a 1:2:2 ratio, with an overall molecular mass of about790 kDa. C1rs is a modular protease with two N-terminal complement C1r/C1s, Uegf and bone morphogenetic protein-1(CUB) domains, separated by an epidermal growth factor (EGF)-ike domain, followed by two complement control modules (CCP) and a C-terminal serine protease (SP) domain Homo sapiens
physiological function the large multicomponent assembly C1 complex, binds to immune complexes, protein modulators (e.g., C-reactive protein), and polyanionic structures on pathogens to initiate complement activation. Binding to pathogens induces a conformational change that drives activation of the zymogen proteases in stepwise fashion: C1r first autoactivates, then activates C1s (2). C1s subsequently cleaves substrates C4 and C4b-bound C2, to form the C3 convertase (C4b2a), the downstream component of the reaction cascade Homo sapiens