2i6q

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spinqualitylabelsall models 2i6q, resolution 2.100Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Complement component C2a

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

C2a provides the catalytic center to the convertase complexes of the, classical and lectin-binding pathways of complement activation. We, determined two crystal structures of full-length C2a, with and without a, pseudo ligand bound. Both structures reveal a near-active conformation of, the catalytic center of the serine protease domains, while the von, Willebrand factor A-type domains display an intermediate activation state, of helix alpha7 with an open, activated metal-ion-dependent adhesion site., The open adhesion site likely serves to enhance the affinity for the, ligand C4b, similar to "inside-out" signaling in integrins. Surprisingly, the N-terminal residues of C2a are buried in a crevice near helix alpha7, indicative of a structural switch between C2 and C2a. Extended loops on, the protease domain possibly envelop the protruding anaphylatoxin domain, of the substrate C3. Together with a putative substrate-induced completion, of the oxyanion hole, this may contribute to the high substrate, specificity of the convertases.

Disease

Known diseases associated with this structure: C2 deficiency OMIM:[217000], Macular degeneration, age-related, reduced risk of OMIM:[217000]

About this Structure

2I6Q is a Single protein structure of sequence from Homo sapiens with NAG, MN and MLI as ligands. Active as Classical-complement-pathway C3/C5 convertase, with EC number 3.4.21.43 Full crystallographic information is available from OCA.

Reference

Structure of complement component C2A: implications for convertase formation and substrate binding., Milder FJ, Raaijmakers HC, Vandeputte MD, Schouten A, Huizinga EG, Romijn RA, Hemrika W, Roos A, Daha MR, Gros P, Structure. 2006 Oct;14(10):1587-97. PMID:17027507

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