1ok2

From Proteopedia

Revision as of 13:52, 30 October 2007

DECAY ACCELERATING FACTOR (CD55): THE STRUCTURE OF AN INTACT HUMAN COMPLEMENT REGULATOR.

Overview

The human complement regulator CD55 is a key molecule protecting, self-cells from complement-mediated lysis. X-ray diffraction and, analytical ultracentrifugation data reveal a rod-like arrangement of four, short consensus repeat (SCR) domains in both the crystal and solution. The, stalk linking the four SCR domains to the glycosylphosphatidylinositol, anchor is extended by the addition of 11 highly charged O-glycans and, positions the domains an estimated 177 A above the membrane. Mutation, mapping and hydrophobic potential analysis suggest that the interaction, with the convertase, and thus complement regulation, depends on the burial, of a hydrophobic patch centered on the linker between SCR domains 2 and 3.

About this Structure

1OK2 is a [Single protein] structure of sequence from [Homo sapiens] with ACT, SO4 and GOL as [ligands]. Structure known Active Site: AC1. Full crystallographic information is available from [OCA].

Reference

Complement regulation at the molecular level: the structure of decay-accelerating factor., Lukacik P, Roversi P, White J, Esser D, Smith GP, Billington J, Williams PA, Rudd PM, Wormald MR, Harvey DJ, Crispin MD, Radcliffe CM, Dwek RA, Evans DJ, Morgan BP, Smith RA, Lea SM, Proc Natl Acad Sci U S A. 2004 Feb 3;101(5):1279-84. Epub 2004 Jan 20. PMID:14734808

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