2c36

From Proteopedia

Revision as of 15:51, 5 November 2007

STRUCTURE OF UNLIGANDED HSV GD REVEALS A MECHANISM FOR RECEPTOR-MEDIATED ACTIVATION OF VIRUS ENTRY

Overview

Herpes simplex virus (HSV) entry into cells requires binding of the, envelope glycoprotein D (gD) to one of several cell surface receptors. The, 50 C-terminal residues of the gD ectodomain are essential for virus entry, but not for receptor binding. We have determined the structure of an, unliganded gD molecule that includes these C-terminal residues. The, structure reveals that the C-terminus is anchored near the N-terminal, region and masks receptor-binding sites. Locking the C-terminus in the, position observed in the crystals by an intramolecular disulfide bond, abolished receptor binding and virus entry, demonstrating that this region, of gD moves upon receptor binding. Similarly, a point mutant that would, destabilize the C-terminus structure was nonfunctional for entry, despite, increased affinity for receptors. We propose that a controlled, displacement of the gD C-terminus upon receptor binding is an essential, feature of HSV entry, ensuring the timely activation of membrane fusion.

About this Structure

2C36 is a Single protein structure of sequence from Human herpesvirus 4 with ZN and CL as ligands. Structure known Active Site: AC1. Full crystallographic information is available from OCA.

Reference

Structure of unliganded HSV gD reveals a mechanism for receptor-mediated activation of virus entry., Krummenacher C, Supekar VM, Whitbeck JC, Lazear E, Connolly SA, Eisenberg RJ, Cohen GH, Wiley DC, Carfi A, EMBO J. 2005 Dec 7;24(23):4144-53. Epub 2005 Nov 17. PMID:16292345

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