1dst
From Proteopedia
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| - | [[Image:1dst.gif|left|200px]] | + | [[Image:1dst.gif|left|200px]] |
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| - | '''MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY''' | + | {{Structure |
| + | |PDB= 1dst |SIZE=350|CAPTION= <scene name='initialview01'>1dst</scene>, resolution 2.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= [http://en.wikipedia.org/wiki/Complement_factor_D Complement factor D], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.46 3.4.21.46] | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1DST is a [ | + | 1DST is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DST OCA]. |
==Reference== | ==Reference== | ||
| - | Crystal structure of a complement factor D mutant expressing enhanced catalytic activity., Kim S, Narayana SV, Volanakis JE, J Biol Chem. 1995 Oct 13;270(41):24399-405. PMID:[http:// | + | Crystal structure of a complement factor D mutant expressing enhanced catalytic activity., Kim S, Narayana SV, Volanakis JE, J Biol Chem. 1995 Oct 13;270(41):24399-405. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/7592653 7592653] |
[[Category: Complement factor D]] | [[Category: Complement factor D]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
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[[Category: serine protease]] | [[Category: serine protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:43:48 2008'' |
Revision as of 08:43, 20 March 2008
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| , resolution 2.0Å | |||||||
|---|---|---|---|---|---|---|---|
| Activity: | Complement factor D, with EC number 3.4.21.46 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
MUTANT OF FACTOR D WITH ENHANCED CATALYTIC ACTIVITY
Contents |
Overview
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.
Disease
Known diseases associated with this structure: Azoospermia OMIM:[400005], Complement factor D deficiency OMIM:[134350], Corneal fleck dystrophy OMIM:[609414], Properdin deficiency, X-linked OMIM:[300383]
About this Structure
1DST is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of a complement factor D mutant expressing enhanced catalytic activity., Kim S, Narayana SV, Volanakis JE, J Biol Chem. 1995 Oct 13;270(41):24399-405. PMID:7592653
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