1i51: Difference between revisions

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-[[Image:1i51.gif|left|200px]]<br />
-<applet load="1i51" size="450" color="white" frame="true" align="right" spinBox="true"
-caption="1i51, resolution 2.45&Aring;" />
-'''CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP'''<br />
-==Overview==
+==CRYSTAL STRUCTURE OF CASPASE-7 COMPLEXED WITH XIAP==
-The inhibitor of apoptosis (IAP) proteins suppress cell death by, inhibiting the catalytic activity of caspases. Here we present the crystal, structure of caspase-7 in complex with a potent inhibitory fragment from, XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic, groove of caspase-7, making extensive contacts to the residues that are, essential for its catalytic activity. Strikingly, despite a reversal of, relative orientation, a subset of interactions between caspase-7 and XIAP, closely resemble those between caspase-7 and its tetrapeptide inhibitor, DEVD-CHO. Our biochemical and structural analyses reveal that the BIR, domains are dispensable for the inhibition of caspase-3 and -7. This study, provides a structural basis for the design of the next-generation caspase, inhibitors.
+<StructureSection load='1i51' size='340' side='right'caption='[[1i51]], [[Resolution|resolution]] 2.45&Aring;' scene=''>
+== Structural highlights ==
+<table><tr><td colspan='2'>[[1i51]] is a 6 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=1I51 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1I51 FirstGlance]. <br>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.45&#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=1i51 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1i51 OCA], [https://pdbe.org/1i51 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1i51 RCSB], [https://www.ebi.ac.uk/pdbsum/1i51 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1i51 ProSAT]</span></td></tr>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/CASP7_HUMAN CASP7_HUMAN] Involved in the activation cascade of caspases responsible for apoptosis execution. Cleaves and activates sterol regulatory element binding proteins (SREBPs). Proteolytically cleaves poly(ADP-ribose) polymerase (PARP) at a '216-Asp-|-Gly-217' bond. Overexpression promotes programmed cell death.
+== 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/i5/1i51_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=1i51 ConSurf].
+<div style="clear:both"></div>
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+The inhibitor of apoptosis (IAP) proteins suppress cell death by inhibiting the catalytic activity of caspases. Here we present the crystal structure of caspase-7 in complex with a potent inhibitory fragment from XIAP at 2.45 A resolution. An 18-residue XIAP peptide binds the catalytic groove of caspase-7, making extensive contacts to the residues that are essential for its catalytic activity. Strikingly, despite a reversal of relative orientation, a subset of interactions between caspase-7 and XIAP closely resemble those between caspase-7 and its tetrapeptide inhibitor DEVD-CHO. Our biochemical and structural analyses reveal that the BIR domains are dispensable for the inhibition of caspase-3 and -7. This study provides a structural basis for the design of the next-generation caspase inhibitors.
-==Disease==
+Structural basis of caspase-7 inhibition by XIAP.,Chai J, Shiozaki E, Srinivasula SM, Wu Q, Datta P, Alnemri ES, Shi Y Cell. 2001 Mar 9;104(5):769-80. PMID:11257230<ref>PMID:11257230</ref>
-Known diseases associated with this structure: Lymphoproliferative syndrome, X-linked, 2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=300079 300079]]
-==About this Structure==
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-I51 is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1I51 OCA].
+</div>
+<div class="pdbe-citations 1i51" style="background-color:#fffaf0;"></div>
-==Reference==
+==See Also==
-Structural basis of caspase-7 inhibition by XIAP., Chai J, Shiozaki E, Srinivasula SM, Wu Q, Datta P, Alnemri ES, Shi Y, Cell. 2001 Mar 9;104(5):769-80. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11257230 11257230]
+*[[Caspase 3D structures|Caspase 3D structures]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
 [[Category: Homo sapiens]]
-[[Category: Protein complex]]
+[[Category: Large Structures]]
-[[Category: Chai, J.]]
+[[Category: Chai J]]
-[[Category: Shi, Y.]]
+[[Category: Shi Y]]
-[[Category: apoptosis]]
-[[Category: caspase]]
-[[Category: iap]]
-[[Category: protease]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 17:26:26 2007''