2c36
From Proteopedia
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==Overview== | ==Overview== | ||
| - | Herpes simplex virus (HSV) entry into cells requires binding of the | + | 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== | ==About this Structure== | ||
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[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Carfi, A.]] | [[Category: Carfi, A.]] | ||
| - | [[Category: Cohen, G | + | [[Category: Cohen, G H.]] |
| - | [[Category: Connolly, S | + | [[Category: Connolly, S A.]] |
| - | [[Category: Eisenberg, R | + | [[Category: Eisenberg, R J.]] |
[[Category: Krummenacher, C.]] | [[Category: Krummenacher, C.]] | ||
[[Category: Lazear, E.]] | [[Category: Lazear, E.]] | ||
| - | [[Category: Supekar, V | + | [[Category: Supekar, V M.]] |
| - | [[Category: Whitbeck, J | + | [[Category: Whitbeck, J C.]] |
| - | [[Category: Wiley, D | + | [[Category: Wiley, D C.]] |
[[Category: CL]] | [[Category: CL]] | ||
[[Category: ZN]] | [[Category: ZN]] | ||
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[[Category: virus]] | [[Category: virus]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:44:22 2008'' |
Revision as of 14:44, 21 February 2008
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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 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 and as ligands. Known structural/functional Site: . 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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