1jvw: Difference between revisions

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 ==TRYPANOSOMA CRUZI MACROPHAGE INFECTIVITY POTENTIATOR (TCMIP)==
-<StructureSection load='1jvw' size='340' side='right' caption='[[1jvw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
+<StructureSection load='1jvw' size='340' side='right'caption='[[1jvw]], [[Resolution|resolution]] 1.70&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1jvw]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Trycr Trycr]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVW OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1JVW FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1jvw]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Trypanosoma_cruzi Trypanosoma cruzi]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JVW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1JVW FirstGlance]. <br>
-</td></tr><tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><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></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.7&#8491;</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=1jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvw OCA], [http://pdbe.org/1jvw PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1jvw RCSB], [http://www.ebi.ac.uk/pdbsum/1jvw PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1jvw ProSAT]</span></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=1jvw FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1jvw OCA], [https://pdbe.org/1jvw PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1jvw RCSB], [https://www.ebi.ac.uk/pdbsum/1jvw PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1jvw ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/MIP_TRYCR MIP_TRYCR]] Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.
+[https://www.uniprot.org/uniprot/MIP_TRYCR MIP_TRYCR] Essential virulence factor associated with macrophage infectivity. Exhibits PPIase activity.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 19: / Line 19: @@
 </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=1jvw ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-The macrophage infectivity potentiator protein from Trypanosoma cruzi (TcMIP) is a major virulence factor secreted by the etiological agent of Chagas' disease. It is functionally involved in host cell invasion. We have determined the three-dimensional crystal structure of TcMIP at 1.7 A resolution. The monomeric protein displays a peptidyl-prolyl cis-trans isomerase (PPIase) core, encompassing the characteristic rotamase hydrophobic active site, thus explaining the strong inhibition of TcMIP by the immunosuppressant FK506 and related drugs. In TcMIP, the twisted beta-sheet of the core is extended by an extra beta-strand, preceded by a long, exposed N-terminal alpha-helix, which might be a target recognition element. An invasion assay shows that the MIP protein from Legionella pneumophila (LpMIP), which has an equivalent N-terminal alpha-helix, can substitute for TcMIP. An additional exposed alpha-helix, this one unique to TcMIP, is located in the C-terminus of the protein. The high-resolution structure reported here opens the possibility for the design of new inhibitory drugs that might be useful for the clinical treatment of American trypanosomiasis.
-Trypanosoma cruzi macrophage infectivity potentiator has a rotamase core and a highly exposed alpha-helix.,Pereira PJ, Vega MC, Gonzalez-Rey E, Fernandez-Carazo R, Macedo-Ribeiro S, Gomis-Ruth FX, Gonzalez A, Coll M EMBO Rep. 2002 Jan;3(1):88-94. Epub 2001 Dec 19. PMID:11751578<ref>PMID:11751578</ref>
+==See Also==
+*[[Peptidyl-prolyl cis-trans isomerase 3D structures|Peptidyl-prolyl cis-trans isomerase 3D structures]]
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1jvw" style="background-color:#fffaf0;"></div>
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Peptidylprolyl isomerase]]
+[[Category: Large Structures]]
-[[Category: Trycr]]
-[[Category: Coll, M]]
-[[Category: Fernandez-Carazo, R]]
-[[Category: Gomis-Rueth, F X]]
-[[Category: Gonzalez, A]]
-[[Category: Gonzalez-Rey, E]]
-[[Category: Macedo-Ribeiro, S]]
-[[Category: Pereira, P J.B]]
-[[Category: Vega, M C]]
-[[Category: Chagas disease]]
-[[Category: Isomerase]]
-[[Category: Macrophage infectivity potentiator]]
-[[Category: Rotamase]]
 [[Category: Trypanosoma cruzi]]
-[[Category: X-ray crystal structure]]
+[[Category: Coll M]]
+[[Category: Fernandez-Carazo R]]
+[[Category: Gomis-Rueth FX]]
+[[Category: Gonzalez A]]
+[[Category: Gonzalez-Rey E]]
+[[Category: Macedo-Ribeiro S]]
+[[Category: Pereira PJB]]
+[[Category: Vega MC]]