2c36

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[[Image:2c36.gif|left|200px]]
[[Image:2c36.gif|left|200px]]
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{{Structure
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|PDB= 2c36 |SIZE=350|CAPTION= <scene name='initialview01'>2c36</scene>, resolution 2.11&Aring;
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The line below this paragraph, containing "STRUCTURE_2c36", creates the "Structure Box" on the page.
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|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+B'>AC1</scene>
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{{STRUCTURE_2c36| PDB=2c36 | SCENE= }}
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2c36 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2c36 OCA], [http://www.ebi.ac.uk/pdbsum/2c36 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=2c36 RCSB]</span>
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'''STRUCTURE OF UNLIGANDED HSV GD REVEALS A MECHANISM FOR RECEPTOR-MEDIATED ACTIVATION OF VIRUS ENTRY'''
'''STRUCTURE OF UNLIGANDED HSV GD REVEALS A MECHANISM FOR RECEPTOR-MEDIATED ACTIVATION OF VIRUS ENTRY'''
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[[Category: Whitbeck, J C.]]
[[Category: Whitbeck, J C.]]
[[Category: Wiley, D C.]]
[[Category: Wiley, D C.]]
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[[Category: glycoprotein]]
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[[Category: Glycoprotein]]
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[[Category: herpes]]
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[[Category: Herpes]]
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[[Category: immunoglobulin-like]]
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[[Category: Immunoglobulin-like]]
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[[Category: transmembrane]]
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[[Category: Transmembrane]]
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[[Category: viral protein]]
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[[Category: Viral protein]]
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[[Category: virus]]
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[[Category: Virus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 21:10:42 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:15:36 2008''
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Revision as of 18:10, 3 May 2008

Template:STRUCTURE 2c36

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 1. 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 Page seeded by OCA on Sat May 3 21:10:42 2008

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