2c36

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|PDB= 2c36 |SIZE=350|CAPTION= <scene name='initialview01'>2c36</scene>, resolution 2.11&Aring;
|PDB= 2c36 |SIZE=350|CAPTION= <scene name='initialview01'>2c36</scene>, resolution 2.11&Aring;
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+B'>AC1</scene>
|SITE= <scene name='pdbsite=AC1:Cl+Binding+Site+For+Chain+B'>AC1</scene>
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|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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|LIGAND= <scene name='pdbligand=BMA:BETA-D-MANNOSE'>BMA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=MAN:ALPHA-D-MANNOSE'>MAN</scene>, <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=NDG:2-(ACETYLAMINO)-2-DEOXY-A-D-GLUCOPYRANOSE'>NDG</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene>
|ACTIVITY=
|ACTIVITY=
|GENE=
|GENE=
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|DOMAIN=
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|RELATEDENTRY=
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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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==About this Structure==
==About this Structure==
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2C36 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_4 Human herpesvirus 4]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C36 OCA].
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2C36 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2C36 OCA].
==Reference==
==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:[http://www.ncbi.nlm.nih.gov/pubmed/16292345 16292345]
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:[http://www.ncbi.nlm.nih.gov/pubmed/16292345 16292345]
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[[Category: Human herpesvirus 4]]
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[[Category: Human herpesvirus 1]]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Carfi, A.]]
[[Category: Carfi, A.]]
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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: CL]]
 
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[[Category: ZN]]
 
[[Category: glycoprotein]]
[[Category: glycoprotein]]
[[Category: herpes]]
[[Category: herpes]]
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[[Category: virus]]
[[Category: virus]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 16:10:09 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 02:15:36 2008''

Revision as of 23:15, 30 March 2008


PDB ID 2c36

Drag the structure with the mouse to rotate
, resolution 2.11Å
Sites:
Ligands: , , , , ,
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



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

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