1awr

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
m (Protected "1awr" [edit=sysop:move=sysop])
Current revision (10:57, 2 August 2023) (edit) (undo)
 
(9 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:1awr.png|left|200px]]
 
-
<!--
+
==CYPA COMPLEXED WITH HAGPIA==
-
The line below this paragraph, containing "STRUCTURE_1awr", creates the "Structure Box" on the page.
+
<StructureSection load='1awr' size='340' side='right'caption='[[1awr]], [[Resolution|resolution]] 1.58&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1awr]] is a 12 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=1AWR OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AWR FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.58&#8491;</td></tr>
-
-->
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1awr FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1awr OCA], [https://pdbe.org/1awr PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1awr RCSB], [https://www.ebi.ac.uk/pdbsum/1awr PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1awr ProSAT]</span></td></tr>
-
{{STRUCTURE_1awr| PDB=1awr | SCENE= }}
+
</table>
 +
== Function ==
 +
[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.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/aw/1awr_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</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=1awr ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
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.
-
===CYPA COMPLEXED WITH HAGPIA===
+
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>
-
 
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
<!--
+
</div>
-
The line below this paragraph, {{ABSTRACT_PUBMED_9385632}}, adds the Publication Abstract to the page
+
<div class="pdbe-citations 1awr" style="background-color:#fffaf0;"></div>
-
(as it appears on PubMed at http://www.pubmed.gov), where 9385632 is the PubMed ID number.
+
-
-->
+
-
{{ABSTRACT_PUBMED_9385632}}
+
-
 
+
-
==About this Structure==
+
-
[[1awr]] is a 12 chain structure of [[Cyclophilin]] with 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=1AWR OCA].
+
==See Also==
==See Also==
-
*[[Cyclophilin]]
+
*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
-
 
+
== References ==
-
==Reference==
+
<references/>
-
<ref group="xtra">PMID:9385632</ref><references group="xtra"/>
+
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Peptidylprolyl isomerase]]
+
[[Category: Large Structures]]
-
[[Category: Vajdos, F F.]]
+
[[Category: Vajdos FF]]
-
[[Category: Cyclophilin some]]
+
-
[[Category: Hiv-1 capsid]]
+
-
[[Category: Pseudo-symmetry]]
+

Current revision

CYPA COMPLEXED WITH HAGPIA

PDB ID 1awr

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1awr"
Personal tools