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1awu

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[[Image:1awu.gif|left|200px]]
 
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{{Structure
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==CYPA COMPLEXED WITH HVGPIA (PSEUDO-SYMMETRIC MONOMER)==
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|PDB= 1awu |SIZE=350|CAPTION= <scene name='initialview01'>1awu</scene>, resolution 2.34&Aring;
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<StructureSection load='1awu' size='340' side='right'caption='[[1awu]], [[Resolution|resolution]] 2.34&Aring;' scene=''>
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|SITE=
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== Structural highlights ==
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|LIGAND=
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<table><tr><td colspan='2'>[[1awu]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AWU FirstGlance]. <br>
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|ACTIVITY= <span class='plainlinks'>[http://en.wikipedia.org/wiki/Peptidylprolyl_isomerase Peptidylprolyl isomerase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=5.2.1.8 5.2.1.8] </span>
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.34&#8491;</td></tr>
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|GENE= CYCLOPHILIN ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1awu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1awu OCA], [https://pdbe.org/1awu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1awu RCSB], [https://www.ebi.ac.uk/pdbsum/1awu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1awu ProSAT]</span></td></tr>
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|DOMAIN=
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</table>
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|RELATEDENTRY=
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== Function ==
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1awu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1awu OCA], [http://www.ebi.ac.uk/pdbsum/1awu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1awu RCSB]</span>
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[https://www.uniprot.org/uniprot/PPIA_HUMAN PPIA_HUMAN] PPIases accelerate the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides.
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}}
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1awu_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1awu ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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The cellular protein, cyclophilin A (CypA), is incorporated into the virion of the type 1 human immunodeficiency virus (HIV-1) via a direct interaction with the capsid domain of the viral Gag polyprotein. We demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92 (87HAGPIA92) encompasses the primary cyclophilin A binding site and present an X-ray crystal structure of the CypA/HAGPIA complex. In contrast to the cis prolines observed in all previously reported structures of CypA complexed with model peptides, the proline in this peptide, Pro 90, binds the cyclophilin A active site in a trans conformation. We also report the crystal structure of a complex between CypA and the hexapeptide HVGPIA, which also maintains the trans conformation. Comparison with the recently determined structures of CypA in complexes with larger fragments of the HIV-1 capsid protein demonstrates that CypA recognition of these hexapeptides involves contacts with peptide residues Ala(Val) 88, Gly 89, and Pro 90, and is independent of the context of longer sequences.
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'''CYPA COMPLEXED WITH HVGPIA (PSEUDO-SYMMETRIC MONOMER)'''
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Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein.,Vajdos FF, Yoo S, Houseweart M, Sundquist WI, Hill CP Protein Sci. 1997 Nov;6(11):2297-307. PMID:9385632<ref>PMID:9385632</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 1awu" style="background-color:#fffaf0;"></div>
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==Overview==
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==See Also==
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The cellular protein, cyclophilin A (CypA), is incorporated into the virion of the type 1 human immunodeficiency virus (HIV-1) via a direct interaction with the capsid domain of the viral Gag polyprotein. We demonstrate that the capsid sequence 87His-Ala-Gly-Pro-Ile-Ala92 (87HAGPIA92) encompasses the primary cyclophilin A binding site and present an X-ray crystal structure of the CypA/HAGPIA complex. In contrast to the cis prolines observed in all previously reported structures of CypA complexed with model peptides, the proline in this peptide, Pro 90, binds the cyclophilin A active site in a trans conformation. We also report the crystal structure of a complex between CypA and the hexapeptide HVGPIA, which also maintains the trans conformation. Comparison with the recently determined structures of CypA in complexes with larger fragments of the HIV-1 capsid protein demonstrates that CypA recognition of these hexapeptides involves contacts with peptide residues Ala(Val) 88, Gly 89, and Pro 90, and is independent of the context of longer sequences.
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*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
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== References ==
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==About this Structure==
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<references/>
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1AWU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AWU OCA].
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__TOC__
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</StructureSection>
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==Reference==
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Crystal structure of cyclophilin A complexed with a binding site peptide from the HIV-1 capsid protein., Vajdos FF, Yoo S, Houseweart M, Sundquist WI, Hill CP, Protein Sci. 1997 Nov;6(11):2297-307. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9385632 9385632]
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
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[[Category: Peptidylprolyl isomerase]]
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[[Category: Large Structures]]
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[[Category: Single protein]]
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[[Category: Vajdos FF]]
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[[Category: Vajdos, F F.]]
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[[Category: complex (isomerase/peptide)]]
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[[Category: cyclophilin some]]
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[[Category: hiv-1 capsid]]
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[[Category: pseudo-symmetry]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:48:58 2008''
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Current revision

CYPA COMPLEXED WITH HVGPIA (PSEUDO-SYMMETRIC MONOMER)

PDB ID 1awu

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