1fgl: Difference between revisions

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-{{Seed}}
-[[Image:1fgl.png|left|200px]]
-<!--
+==Cyclophilin A complexed with a fragment of HIV-1 GAG protein==
-The line below this paragraph, containing "STRUCTURE_1fgl", creates the "Structure Box" on the page.
+<StructureSection load='1fgl' size='340' side='right'caption='[[1fgl]], [[Resolution|resolution]] 1.80&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'>[[1fgl]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] and [https://en.wikipedia.org/wiki/Human_immunodeficiency_virus_type_1_(WMJ2_ISOLATE) Human immunodeficiency virus type 1 (WMJ2 ISOLATE)]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FGL OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FGL 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]] 1.8&#8491;</td></tr>
--->
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=BAL:BETA-ALANINE'>BAL</scene>, <scene name='pdbligand=NLE:NORLEUCINE'>NLE</scene></td></tr>
-{{STRUCTURE_1fgl|  PDB=1fgl  |  SCENE=  }}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1fgl FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fgl OCA], [https://pdbe.org/1fgl PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fgl RCSB], [https://www.ebi.ac.uk/pdbsum/1fgl PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fgl ProSAT]</span></td></tr>
+</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/fg/1fgl_consurf.spt"</scriptWhenChecked>
+    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.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=1fgl ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+BACKGROUND: Cyclophilin A (CyPA), a receptor of the immunosuppressive drug cyclosporin A, catalyzes the cis-trans isomerization of peptidyl-prolyl bonds and is required for the infectious activity of human immunodeficiency virus type 1 (HIV-1). The crystal structure of CyPA complexed with a fragment of the HIV-1 gag protein should provide insights into the nature of CyPA-gag interactions and may suggest a role for CyPA in HIV-1 infectious activity. RESULTS: The crystal structure of CyPA complexed with a 25 amino acid peptide of HIV-1 gag capsid protein (25-mer) was determined and refined to an R factor of 0.195 at 1.8 A resolution. The sequence Ala88-Gly89-Pro90-Ile91 of the gag fragment is the major portion to bind to the active site of CyPA. Two residues of the 25-mer (Pro90-Ile91) bind to CyPA in a similar manner to two residues (Pro-Phe) of the CyPA substrate, succinyl-Ala-Ala-Pro-Phe-p-nitroanilide (AAPF). However, the N-terminus of the 25-mer (Ala88-Gly89) exhibits a different hydrogen-bonding pattern and molecular conformation than AAPF. The peptidyl-prolyl bond between Gly89 and Pro90 of the 25-mer has a trans conformation, in contrast to the cis conformation observed in other known CyPA-peptide complexes. The residue preceding proline, Gly89, has an unfavorable backbone conformation usually only adopted by glycine. CONCLUSIONS: The unfavorable backbone conformation of Gly89 of the gag 25-mer fragment suggests that binding between HIV-1 gag protein and CyPA requires a special sequence, Gly-Pro. Thus, in HIV-1 infectivity, CyPA is likely to function as a chaperone, rather than as a cis-trans isomerase. However, the observation of similarities between the C termini of the 25-mer and the substrate AAPF means that the involvement of the cis-trans isomerase activity of CyPA cannot be completely ruled out.
-===CYCLOPHILIN A COMPLEXED WITH A FRAGMENT OF HIV-1 GAG PROTEIN===
+Cyclophilin A complexed with a fragment of HIV-1 gag protein: insights into HIV-1 infectious activity.,Zhao Y, Chen Y, Schutkowski M, Fischer G, Ke H Structure. 1997 Jan 15;5(1):139-46. PMID:9016720<ref>PMID:9016720</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 1fgl" style="background-color:#fffaf0;"></div>
-<!--
+==See Also==
-The line below this paragraph, {{ABSTRACT_PUBMED_9016720}}, adds the Publication Abstract to the page
+*[[Cyclophilin 3D structures|Cyclophilin 3D structures]]
-(as it appears on PubMed at http://www.pubmed.gov), where 9016720 is the PubMed ID number.
+*[[Gag polyprotein 3D structures|Gag polyprotein 3D structures]]
--->
+== References ==
-{{ABSTRACT_PUBMED_9016720}}
+<references/>
+__TOC__
-==About this Structure==
+</StructureSection>
-FGL is a [[Protein complex]] structure of sequences 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=1FGL OCA].
-==Reference==
-Cyclophilin A complexed with a fragment of HIV-1 gag protein: insights into HIV-1 infectious activity., Zhao Y, Chen Y, Schutkowski M, Fischer G, Ke H, Structure. 1997 Jan 15;5(1):139-46. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9016720 9016720]
 [[Category: Homo sapiens]]
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Large Structures]]
-[[Category: Protein complex]]
+[[Category: Chen Y]]
-[[Category: Chen, Y.]]
+[[Category: Fischer G]]
-[[Category: Fischer, G.]]
+[[Category: Ke H]]
-[[Category: Ke, H.]]
+[[Category: Schutkowski M]]
-[[Category: Schutkowski, M.]]
+[[Category: Zhao Y]]
-[[Category: Zhao, Y.]]
-[[Category: Aid]]
-[[Category: Binding protein for cyclosporin some]]
-[[Category: Cyclophilin]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 03:13:07 2008''