3HQB
Crystal structure of human desarg-C5A
Summary for 3HQB
| Entry DOI | 10.2210/pdb3hqb/pdb |
| Related | 3HQA |
| Descriptor | Complement C5 (1 entity in total) |
| Functional Keywords | complement, c5a, anaphylatoxin, cleavage on pair of basic residues, complement alternate pathway, complement pathway, cytolysis, disulfide bond, glycoprotein, immune response, inflammatory response, innate immunity, membrane attack complex, secreted, immune system |
| Biological source | Homo sapiens (human) |
| Total number of polymer chains | 2 |
| Total formula weight | 16323.15 |
| Authors | Cook, W.J.,Ealick, S.E. (deposition date: 2009-06-05, release date: 2010-02-02, Last modification date: 2024-11-20) |
| Primary citation | Cook, W.J.,Galakatos, N.,Boyar, W.C.,Walter, R.L.,Ealick, S.E. Structure of human desArg-C5a. Acta Crystallogr.,Sect.D, 66:190-197, 2010 Cited by PubMed Abstract: The anaphylatoxin C5a is derived from the complement component C5 during activation of the complement cascade. It is an important component in the pathogenesis of a number of inflammatory diseases. NMR structures of human and porcine C5a have been reported; these revealed a four-helix bundle stabilized by three disulfide bonds. The crystal structure of human desArg-C5a has now been determined in two crystal forms. Surprisingly, the protein crystallizes as a dimer and each monomer in the dimer has a three-helix core instead of the four-helix bundle noted in the NMR structure determinations. Furthermore, the N-terminal helices of the two monomers occupy different positions relative to the three-helix core and are completely different from the NMR structures. The physiological significance of these structural differences is unknown. PubMed: 20124699DOI: 10.1107/S0907444909049051 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (3.299 Å) |
Structure validation
Download full validation report
