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3ds2

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Revision as of 08:55, 25 October 2017

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

Structural highlights

3ds2 is a 2 chain structure with sequence from Hiv-1. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Related:	3ds4, 3ds3, 3dtj, 3ds1, 3ds5, 3ds0, 3dph
Gene:	gag (HIV-1)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[Q72497_9HIV1] Capsid protein p24 forms the conical core of the virus that encapsulates the genomic RNA-nucleocapsid complex (By similarity). Nucleocapsid protein p7 encapsulates and protects viral dimeric unspliced (genomic) RNA. Binds these RNAs through its zinc fingers (By similarity).[SAAS:SAAS012344_004_011858]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Morphogenesis of infectious HIV-1 involves budding of immature virions followed by proteolytic disassembly of the Gag protein shell and subsequent assembly of processed capsid proteins (CA) into the mature HIV-1 core. The dimeric interface between C-terminal domains of CA (C-CA) has been shown to be important for both immature and mature assemblies. We previously reported a CA-binding peptide (CAI) that blocks both assembly steps in vitro. The three-dimensional structure of the C-CA/CAI complex revealed an allosteric effect of CAI that alters the C-CA dimer interface. Based on this structure, we now investigated the phenotypes of mutations in the binding pocket. CA variants carrying mutations Y169A, L211A, or L211S had a reduced affinity for CAI and were unable to form mature-like particles in vitro. These mutations also blocked morphological conversion to mature virions in tissue culture and abolished infectivity. X-ray crystallographic analyses of the variant C-CA domains revealed that these alterations induced the same allosteric change at the dimer interface observed in the C-CA/CAI complex. These results point to a role of key interactions between conserved amino acids in the CAI binding pocket of C-CA in maintaining the correct conformation necessary for mature core assembly.

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:18772135^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ 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

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/3ds2"

@@ Line 1: / Line 1: @@
 ==HIV-1 capsid C-terminal domain mutant (Y169A)==
 <StructureSection load='3ds2' size='340' side='right' caption='[[3ds2]], [[Resolution|resolution]] 1.20&Aring;' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3ds4|3ds4]], [[3ds3|3ds3]], [[3dtj|3dtj]], [[3ds1|3ds1]], [[3ds5|3ds5]], [[3ds0|3ds0]], [[3dph|3dph]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">gag ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11698 HIV-1])</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ds2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ds2 OCA], [http://pdbe.org/3ds2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ds2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ds2 PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3ds2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3ds2 OCA], [http://pdbe.org/3ds2 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3ds2 RCSB], [http://www.ebi.ac.uk/pdbsum/3ds2 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3ds2 ProSAT]</span></td></tr>
 </table>
 == Function ==
@@ Line 28: / Line 29: @@
 </div>
 <div class="pdbe-citations 3ds2" style="background-color:#fffaf0;"></div>
-==See Also==
-*[[Virus coat protein|Virus coat protein]]
 == References ==
 <references/>
@@ Line 38: / Line 36: @@
 [[Category: Igonet, S]]
 [[Category: Rey, F A]]
-[[Category: Vaney,M C]]
+[[Category: Vaney, M C]]
 [[Category: Assembly]]
 [[Category: Capsid]]

3ds2

From Proteopedia

Revision as of 08:55, 25 October 2017

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

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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