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2a73

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This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

2a73, resolution 3.30Å ()

Non-Standard Residues:

, ,

Domains:

A2M_N, A2M_N_2, NTR_complement_C3, A2M_recep, complement_C3_C4_C5, A2M, ANATO, A2M_comp

Structural annotation:
Resources:	InterPro : Ipr001840, Ipr008930, Ipr008993, Ipr009048, Ipr002890, Ipr001134, Ipr011626, Ipr011625, Ipr001599, Ipr000020 Pfam : PF01835, PF07703, PF01821, PF01759, PF00207, PF07678, PF07677 UniProt : P01024

Functional annotation:
Resources:	GeneCard : C3
Cellular component:	extracellular region
Biological process:	complement activation, alternative pathway immune response signal transduction innate immune response complement activation, classical pathway positive regulation of type IIa hypersensitivity inflammatory response positive regulation of phagocytosis complement activation G-protein coupled receptor protein signaling pathway
Molecular function:	receptor binding protein binding endopeptidase inhibitor activity

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

Human Complement Component C3

Publication Abstract from PubMed

The mammalian complement system is a phylogenetically ancient cascade system that has a major role in innate and adaptive immunity. Activation of component C3 (1,641 residues) is central to the three complement pathways and results in inflammation and elimination of self and non-self targets. Here we present crystal structures of native C3 and its final major proteolytic fragment C3c. The structures reveal thirteen domains, nine of which were unpredicted, and suggest that the proteins of the alpha2-macroglobulin family evolved from a core of eight homologous domains. A double mechanism prevents hydrolysis of the thioester group, essential for covalent attachment of activated C3 to target surfaces. Marked conformational changes in the alpha-chain, including movement of a critical interaction site through a ring formed by the domains of the beta-chain, indicate an unprecedented, conformation-dependent mechanism of activation, regulation and biological function of C3.

Structures of complement component C3 provide insights into the function and evolution of immunity., Janssen BJ, Huizinga EG, Raaijmakers HC, Roos A, Daha MR, Nilsson-Ekdahl K, Nilsson B, Gros P, Nature. 2005 Sep 22;437(7058):505-11. PMID:16177781

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

2A73 is a 2 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Janssen BJ, Huizinga EG, Raaijmakers HC, Roos A, Daha MR, Nilsson-Ekdahl K, Nilsson B, Gros P. Structures of complement component C3 provide insights into the function and evolution of immunity. Nature. 2005 Sep 22;437(7058):505-11. PMID:16177781 doi:10.1038/nature04005

Page seeded by OCA on Tue Feb 17 00:19:43 2009

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2a73

From Proteopedia

Human Complement Component C3

About this Structure

Reference

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