2c36
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(New page: 200px<br /> <applet load="2c36" size="450" color="white" frame="true" align="right" spinBox="true" caption="2c36, resolution 2.11Å" /> '''STRUCTURE OF UNLIGA...)
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Revision as of 16:52, 29 October 2007
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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, ... [(full description)]
About this Structure
2C36 is a [Single protein] structure of sequence from [Human herpesvirus 1] with ZN and CL as [ligands]. 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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