3ds2

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==Reference==
==Reference==
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Residues in the HIV-1 Capsid Assembly Inhibitor Binding Site Are Essential for Maintaining the Assembly-competent Quaternary Structure of the Capsid Protein., Bartonova V, Igonet S, Sticht J, Glass B, Habermann A, Vaney MC, Sehr P, Lewis J, Rey FA, Krausslich HG, J Biol Chem. 2008 Nov 14;283(46):32024-33. Epub 2008 Sep 4. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/18772135 18772135]
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<ref group="xtra">PMID:18772135</ref><ref group="xtra">PMID:16041386</ref><references group="xtra"/>
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The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor., Ternois F, Sticht J, Duquerroy S, Krausslich HG, Rey FA, Nat Struct Mol Biol. 2005 Aug;12(8):678-82. Epub 2005 Jul 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/16041386 16041386]
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[[Category: Human immunodeficiency virus 1]]
[[Category: Human immunodeficiency virus 1]]
[[Category: Igonet, S.]]
[[Category: Igonet, S.]]
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[[Category: Viral protein]]
[[Category: Viral protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Nov 27 13:52:40 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 10:35:31 2009''

Revision as of 08:35, 17 February 2009

Template:STRUCTURE 3ds2

HIV-1 capsid C-terminal domain mutant (Y169A)

Template:ABSTRACT PUBMED 18772135

About this Structure

3DS2 is a 2 chains structure of sequences from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.

Reference

  • Bartonova V, Igonet S, Sticht J, Glass B, Habermann A, Vaney MC, Sehr P, Lewis J, Rey FA, Krausslich HG. Residues in the HIV-1 capsid assembly inhibitor binding site are essential for maintaining the assembly-competent quaternary structure of the capsid protein. J Biol Chem. 2008 Nov 14;283(46):32024-33. Epub 2008 Sep 4. PMID:18772135 doi:10.1074/jbc.M804230200
  • Ternois F, Sticht J, Duquerroy S, Krausslich HG, Rey FA. The HIV-1 capsid protein C-terminal domain in complex with a virus assembly inhibitor. Nat Struct Mol Biol. 2005 Aug;12(8):678-82. Epub 2005 Jul 24. PMID:16041386 doi:10.1038/nsmb967

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