1DST
MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY
Summary for 1DST
| Entry DOI | 10.2210/pdb1dst/pdb |
| Descriptor | FACTOR D (2 entities in total) |
| Functional Keywords | complement activating enzyme, hydrolase, serine protease, factor d, hydrolase (serine protease) |
| Biological source | Homo sapiens (human) |
| Cellular location | Secreted: P00746 |
| Total number of polymer chains | 1 |
| Total formula weight | 24600.01 |
| Authors | Narayana, S.V.L.,Volanakis, J.E. (deposition date: 1995-09-13, release date: 1996-07-11, Last modification date: 2024-10-16) |
| Primary citation | Kim, S.,Narayana, S.V.,Volanakis, J.E. Crystal structure of a complement factor D mutant expressing enhanced catalytic activity. J.Biol.Chem., 270:24399-24405, 1995 Cited by PubMed Abstract: Complement factor D is a serine protease regulated by a novel mechanism that depends on conformational changes rather than cleavage of a zymogen for expression of proteolytic activity. The conformational changes are presumed to be induced by the single natural substrate, C3bB, and to result in reversible reorientation of the catalytic center and of the substrate binding site of factor D, both of which have atypical conformations. Here we report that replacement of Ser94, Thr214, and Ser215 of factor D (chymotrypsinogen numbering has been used for comparison purposes) with the corresponding residues of trypsin, Tyr, Ser, and Trp, is sufficient to induce substantially higher catalytic activity associated with a typical serine protease alignment of the catalytic triad residues His57, Asp102, and Ser195. These results provide a partial structural explanation for the low reactivity of "resting-state" factor D toward synthetic substrates. PubMed: 7592653DOI: 10.1074/jbc.270.41.24399 PDB entries with the same primary citation |
| Experimental method | X-RAY DIFFRACTION (2 Å) |
Structure validation
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