2XWB
Crystal Structure of Complement C3b in complex with Factors B and D
Summary for 2XWB
| Entry DOI | 10.2210/pdb2xwb/pdb |
| Related | 1BIO 1C3D 1DFP 1DIC 1DLE 1DST 1DSU 1FDP 1GHQ 1HFD 1Q0P 1RRK 1RS0 1RTK 1W2S 2A73 2A74 2HR0 2WII 2WIN 2WY7 2WY8 2XQW 2XW9 2XWA 2XWJ |
| Descriptor | COMPLEMENT C3B BETA CHAIN, COMPLEMENT C3B ALPHA' CHAIN, COMPLEMENT FACTOR B, ... (10 entities in total) |
| Functional Keywords | immune system, pro-convertase, hydrolase, serine protease, conformational changes, alternative pathway |
| Biological source | HOMO SAPIENS (HUMAN) More |
| Cellular location | Secreted: P01024 P01024 P00751 P00746 |
| Total number of polymer chains | 8 |
| Total formula weight | 566820.38 |
| Authors | Forneris, F.,Ricklin, D.,Wu, J.,Tzekou, A.,Wallace, R.S.,Lambris, J.D.,Gros, P. (deposition date: 2010-11-01, release date: 2011-01-12, Last modification date: 2024-11-13) |
| Primary citation | Forneris, F.,Ricklin, D.,Wu, J.,Tzekou, A.,Wallace, R.S.,Lambris, J.D.,Gros, P. Structures of C3B in Complex with Factors B and D Give Insight Into Complement Convertase Formation. Science, 330:1816-, 2010 Cited by PubMed Abstract: Activation of the complement cascade induces inflammatory responses and marks cells for immune clearance. In the central complement-amplification step, a complex consisting of surface-bound C3b and factor B is cleaved by factor D to generate active convertases on targeted surfaces. We present crystal structures of the pro-convertase C3bB at 4 angstrom resolution and its complex with factor D at 3.5 angstrom resolution. Our data show how factor B binding to C3b forms an open "activation" state of C3bB. Factor D specifically binds the open conformation of factor B through a site distant from the catalytic center and is activated by the substrate, which displaces factor D's self-inhibitory loop. This concerted proteolytic mechanism, which is cofactor-dependent and substrate-induced, restricts complement amplification to C3b-tagged target cells. PubMed: 21205667DOI: 10.1126/SCIENCE.1195821 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.49 Å) |
Structure validation
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