1dic

From Proteopedia

Revision as of 12:56, 30 October 2007

STRUCTURE OF 3,4-DICHLOROISOCOUMARIN-INHIBITED FACTOR D

Overview

Factor D (D) is a serine protease essential in the activation of the, alternative complement pathway. Only a few of the common serine protease, inhibitors inhibit D, binding covalently to the serine hydroxyl of the, catalytic triad. 3,4-Dichloroisocoumarin (DCI) is a mechanism-based, inhibitor which inhibits most serine proteases and many esterases, including D. The structure of the enzyme:inhibitor covalent adduct of D, with DCI, DCI:D, to a resolution of 1.8 A is described, which represents, the first structural analysis of D with a mechanism-based inhibitor. The, side chain of the ring-opened DCI moiety of the protein adduct undergoes, chemical modification in the buffered solution, resulting in the formation, of an alpha-hydroxy acid moiety through the nucleophilic substitution of, ... [(full description)]

About this Structure

1DIC is a [Single protein] structure of sequence from [Homo sapiens] with DIC and O as [ligands]. Active as [Complement factor D], with EC number [3.4.21.46]. Structure known Active Site: S1. Full crystallographic information is available from [OCA].

Reference

Structure of 3,4-dichloroisocoumarin-inhibited factor D., Cole LB, Kilpatrick JM, Chu N, Babu YS, Acta Crystallogr D Biol Crystallogr. 1998 Sep 1;54(Pt 5):711-7. PMID:9757085

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