1dsu

From Proteopedia

HUMAN FACTOR D, COMPLEMENT ACTIVATING ENZYME

Overview

Factor D, an essential enzyme for the activation of the alternative, pathway of the complement system, belongs to the serine protease, superfamily. The crystal structure of the enzyme was solved by a, combination of multiple isomorphous replacement and molecular replacement, methods. The present model was refined to an R-factor of 18.8% using, 23,681 observed reflections between 7.5 and 2.0 A resolution, with a, root-mean-square deviation from standard bond lengths of 0.016 A. The two, non-crystallographically related molecules in the triclinic unit cell have, distinctive active site conformations. The protein has the general, structural fold of a serine protease, but there are several unique amino, acid substitutions resulting in significant alterations in the critical, loops responsible for catalysis and substrate specificity in serine, proteases. Factor D is the first complement serine protease whose, three-dimensional structure has been determined.

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

1DSU is a Single protein structure of sequence from Homo sapiens. Active as Complement factor D, with EC number 3.4.21.46 Full crystallographic information is available from OCA.

Reference

Structure of human factor D. A complement system protein at 2.0 A resolution., Narayana SV, Carson M, el-Kabbani O, Kilpatrick JM, Moore D, Chen X, Bugg CE, Volanakis JE, DeLucas LJ, J Mol Biol. 1994 Jan 14;235(2):695-708. PMID:8289289

Page seeded by OCA on Mon Nov 12 16:35:27 2007