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monomer
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1 * isolated GTPase domain, SDS-PAGE
oligomer
in solution, Drp1 exists in a number of oligomeric states, including dimers, tetramers, and higher-order oligomers. Actin filaments can organize Drp1 into a productive oligomer
?
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x * 100000, about, Western blot analysis
?
x * 40923, nucleotide-free GTPase-GTPase effector domain fusion protein of Drp1, mass spectrometry
dimer
2 * 78000-85000, recombinant enzyme, SDS-PAGE
dimer
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Sey1p undergoes GTP-dependent dimerization
heterotetramer
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Dyn1 can interfere with Dyn2 or Dyn2 mutants, Dyn2-Dyn1, Dyn2S45N-Dyn1 and Dyn2-Dyn1I690K heteromers are formed
heterotetramer
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Dyn2 can interfere with Dyn2 mutants or Dyn1, Dyn2-Dyn1, Dyn2S45N-Dyn1 and Dyn2-Dyn1I690K heteromers are formed
homotetramer
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tetramer
dimer of dimers, 4 * 39000, crystal structure analysis
tetramer
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a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions
tetramer
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a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions
tetramer
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4 * 80000, SDS-PAGE, 4 * 45000, isolated PH-like domain, SDS-PAGE
tetramer
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a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions. The tetrameric form of dynamin, which can be abundant in solution, may be an intermediate in higher-order assembly
tetramer
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a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions. The tetrameric form of dynamin, which can be abundant in solution, may be an intermediate in higher-order assembly
tetramer
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dynamin dimers need to oligomerize into tetramers for efficient GTP binding
tetramer
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a dimer of dimers, the stalk of dynamin dimerizes in a cross-like fashion to yield a dynamin dimer in which the two G domains are oriented in opposite directions. The tetrameric form of dynamin, which can be abundant in solution, may be an intermediate in higher-order assembly
additional information
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dynamin is characterized by a tetramer/monomer equilibrium. Dynamin molecules must be in proper conformation or orientation if they are to form an active oligomer
additional information
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oligomerization of dynamin stimulates its GTPase activity
additional information
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structure-function relationship, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
enzyme Sey1p forms a side-by-side dimer in complex with GMP-PNP or GDP/AIF4-, but is monomeric with GDP. The dimerization of caSey1p involves a hydrophobic patch on top of the GTPase domain, including a conserved L257 within the guanine cap, and several hydrophilic interactions along the GTPase interface. The stalk domains also pack against each other in the dimer
additional information
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enzyme Sey1p forms a side-by-side dimer in complex with GMP-PNP or GDP/AIF4-, but is monomeric with GDP. The dimerization of caSey1p involves a hydrophobic patch on top of the GTPase domain, including a conserved L257 within the guanine cap, and several hydrophilic interactions along the GTPase interface. The stalk domains also pack against each other in the dimer
additional information
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structure-function relationship, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
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dynamin can self-assemble forming higher order structures such as rings and spirals that exhibit up to 100fold stimulated GTPase activity
additional information
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oligomerization (large soluble oligomers with a molecular mass of 600000 da) is mediated by the GTPase effector domain. Structural characterization of the large soluble oligomers of the GTPase effector domain of dynamin
additional information
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DLP-1 contains a GTPase domain, a middle domain, a putative PH-like domain, and a GTPase effector domain, GED
additional information
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structure-function relationship, overview. Dynamin polymerization results from the apposition of dimers via stalk-tip interactions, mechanism, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
dimerization of MxA via a GTPase domain interface is required for GTP hydrolysis and antiviral activity. Residues in the catalytic center of MxA and the nucleotide itself are essential for G domain dimerization and catalytic activation
additional information
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dimerization of MxA via a GTPase domain interface is required for GTP hydrolysis and antiviral activity. Residues in the catalytic center of MxA and the nucleotide itself are essential for G domain dimerization and catalytic activation
additional information
dynamin 2 is a multidomain protein composed of an N-terminal GTPase domain, a middle domain (MID), a pleckstrin homology (PH) domain, a GTPase effector domain (GED), and a C-terminal prolinearginine-rich domain (PRD)
additional information
all dynamin isoforms share similar domain structures aligned from N-terminus to C-terminus: a GTPase domain, a middle domain, a PH domain, a GTPase effector domain (GED) and PRD domain
additional information
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all dynamin isoforms share similar domain structures aligned from N-terminus to C-terminus: a GTPase domain, a middle domain, a PH domain, a GTPase effector domain (GED) and PRD domain
additional information
Drp1 isoforms exhibit differential oligomerization propensities in solution and distinct helical geometry on cardiolipin-containing membranes, analysis of Drp1-short, Drp1-A-only, and Drp1-B-only by gel filtration
additional information
dynamin can be subdivided into five domains: the N-terminal GTPase domain (G domain), the bundle signalling element (BSE), the stalk, the pleckstrin homology domain (PH domain), and the proline-rich domain (PRD). The G domain binds and hydrolyses GTP. The BSE is a three-helix bundle originating from the termini of the G domain and from a more C-terminal helix that fold back towards the N-terminus
additional information
enzyme domain structure, overview. Hydrogen-deuterium exchange kinetics reveal long-range nucleotide- and/or membrane-binding-driven conformational changes in dynamin
additional information
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structure-function relationship, overview. Dynamin polymerization results from the apposition of dimers via stalk-tip interactions, mechanism, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
the enzyme's middle domain is involved in the formation of functional oligomers. Wild-type enzyme forms oligomers, while enzyme mutant R386G prefers to form monomers
additional information
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assembly into higher order structures such as rings or spirals
additional information
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dynamin is a multidomain protein that self-assembles into higher order structures resembling rings during endocytosis
additional information
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structure-function relationship, overview. Dynamin polymerization results from the apposition of dimers via stalk-tip interactions, mechanism, overview. Domain organization, dynamin has an N-terminal G domain, a middle or stalk region, a pleckstrin homology PH domain, a GTPase effector domain GED, interacting with the G domain, and a C-terminal Pro-rich region, PRD
additional information
all dynamin isoforms share similar domain structures aligned from N-terminus to C-terminus: a GTPase domain, a middle domain, a PH domain, a GTPase effector domain (GED) and proline/arginine-rich domain (PRD) domain
additional information
Drp1 isoforms exhibit differential oligomerization propensities in solution and distinct helical geometry on cardiolipin-containing membranes, analysis of Drp1-long, Drp1-A-only, and Drp1-B-only by gel filtration
additional information
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Sey1p dimerizes in the presence of GDP AlFx