2odp
From Proteopedia
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|PDB= 2odp |SIZE=350|CAPTION= <scene name='initialview01'>2odp</scene>, resolution 1.900Å | |PDB= 2odp |SIZE=350|CAPTION= <scene name='initialview01'>2odp</scene>, resolution 1.900Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand= | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene> |
| - | |ACTIVITY= [http://en.wikipedia.org/wiki/Classical-complement-pathway_C3/C5_convertase Classical-complement-pathway C3/C5 convertase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.43 3.4.21.43] | + | |ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Classical-complement-pathway_C3/C5_convertase Classical-complement-pathway C3/C5 convertase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.43 3.4.21.43] </span> |
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[2odq|2ODQ]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2odp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2odp OCA], [http://www.ebi.ac.uk/pdbsum/2odp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2odp RCSB]</span> | ||
}} | }} | ||
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==Overview== | ==Overview== | ||
The multi-domain serine protease C2 provides the catalytic activity for the C3 and C5- convertases of the classical and lectin pathways of complement activation. Formation of these convertases requires the Mg(2+)-dependent binding of C2 to C4b, and the subsequent cleavage of C2 by C1s or MASP2, respectively. The C-terminal fragment C2a consisting of a serine protease (SP) and a von Willebrand factor type A (vWFA) domain, remains attached to C4b, forming the C3 convertase, C4b2a. Here, we present the crystal structure of Mg(2+)-bound C2a to 1.9 A resolution in comparison to its homolog Bb, the catalytic subunit of the alternative pathway C3 convertase, C3bBb. Although the overall domain arrangement of C2a is similar to Bb, there are certain structural differences. Unexpectedly, the conformation of the metal ion-dependent adhesion site and the position of the alpha7 helix of the vWFA domain indicate a co-factor-bound or open conformation. The active site of the SP domain is in a zymogen-like inactive conformation. On the basis of these structural features, we suggest a model for the initial steps of C3 convertase assembly. | The multi-domain serine protease C2 provides the catalytic activity for the C3 and C5- convertases of the classical and lectin pathways of complement activation. Formation of these convertases requires the Mg(2+)-dependent binding of C2 to C4b, and the subsequent cleavage of C2 by C1s or MASP2, respectively. The C-terminal fragment C2a consisting of a serine protease (SP) and a von Willebrand factor type A (vWFA) domain, remains attached to C4b, forming the C3 convertase, C4b2a. Here, we present the crystal structure of Mg(2+)-bound C2a to 1.9 A resolution in comparison to its homolog Bb, the catalytic subunit of the alternative pathway C3 convertase, C3bBb. Although the overall domain arrangement of C2a is similar to Bb, there are certain structural differences. Unexpectedly, the conformation of the metal ion-dependent adhesion site and the position of the alpha7 helix of the vWFA domain indicate a co-factor-bound or open conformation. The active site of the SP domain is in a zymogen-like inactive conformation. On the basis of these structural features, we suggest a model for the initial steps of C3 convertase assembly. | ||
| - | |||
| - | ==Disease== | ||
| - | Known diseases associated with this structure: C2 deficiency OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=217000 217000]], Macular degeneration, age-related, reduced risk of OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=217000 217000]] | ||
==About this Structure== | ==About this Structure== | ||
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[[Category: Krishnan, V.]] | [[Category: Krishnan, V.]] | ||
[[Category: Narayana, S V.L.]] | [[Category: Narayana, S V.L.]] | ||
| - | [[Category: MG]] | ||
| - | [[Category: NAG]] | ||
[[Category: c3/c5 convertase]] | [[Category: c3/c5 convertase]] | ||
[[Category: complement component c2a]] | [[Category: complement component c2a]] | ||
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[[Category: vwfa]] | [[Category: vwfa]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 04:16:15 2008'' |
Revision as of 01:16, 31 March 2008
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| , resolution 1.900Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | , | ||||||
| Activity: | Classical-complement-pathway C3/C5 convertase, with EC number 3.4.21.43 | ||||||
| Related: | 2ODQ
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Complement component C2a, the catalytic fragment of C3- and C5-convertase of human complement
Overview
The multi-domain serine protease C2 provides the catalytic activity for the C3 and C5- convertases of the classical and lectin pathways of complement activation. Formation of these convertases requires the Mg(2+)-dependent binding of C2 to C4b, and the subsequent cleavage of C2 by C1s or MASP2, respectively. The C-terminal fragment C2a consisting of a serine protease (SP) and a von Willebrand factor type A (vWFA) domain, remains attached to C4b, forming the C3 convertase, C4b2a. Here, we present the crystal structure of Mg(2+)-bound C2a to 1.9 A resolution in comparison to its homolog Bb, the catalytic subunit of the alternative pathway C3 convertase, C3bBb. Although the overall domain arrangement of C2a is similar to Bb, there are certain structural differences. Unexpectedly, the conformation of the metal ion-dependent adhesion site and the position of the alpha7 helix of the vWFA domain indicate a co-factor-bound or open conformation. The active site of the SP domain is in a zymogen-like inactive conformation. On the basis of these structural features, we suggest a model for the initial steps of C3 convertase assembly.
About this Structure
2ODP is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
The crystal structure of C2a, the catalytic fragment of classical pathway C3 and C5 convertase of human complement., Krishnan V, Xu Y, Macon K, Volanakis JE, Narayana SV, J Mol Biol. 2007 Mar 16;367(1):224-33. Epub 2006 Dec 19. PMID:17234210
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