1f1j: Difference between revisions

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-[[Image:1f1j.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHO==
-|PDB= 1f1j |SIZE=350|CAPTION= <scene name='initialview01'>1f1j</scene>, resolution 2.35&Aring;
+<StructureSection load='1f1j' size='340' side='right'caption='[[1f1j]], [[Resolution|resolution]] 2.35&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene>
+<table><tr><td colspan='2'>[[1f1j]] is a 4 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The August 2004 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Caspases''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2004_8 10.2210/rcsb_pdb/mom_2004_8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1J OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1F1J FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.35&#8491;</td></tr>
-|GENE=
+<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=ASJ:(3S)-3-AMINO-4-HYDROXYBUTANOIC+ACID'>ASJ</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></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=1f1j FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1f1j OCA], [https://pdbe.org/1f1j PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1f1j RCSB], [https://www.ebi.ac.uk/pdbsum/1f1j PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1f1j 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/f1/1f1j_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=1f1j ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF CASPASE-7 IN COMPLEX WITH ACETYL-ASP-GLU-VAL-ASP-CHO'''
+==See Also==
+*[[Caspase 3D structures|Caspase 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-BACKGROUND: Peptide inhibitors of caspases have helped define the role of these cysteine proteases in biology. Structural and biochemical characterization of the caspase enzymes may contribute to the development of new drugs for the treatment of caspase-mediated inflammation and apoptosis. RESULTS: The crystal structure of the previously unpublished caspase-7 (Csp7; 2.35 A) bound to the reversible tetrapeptide aldehyde inhibitor acetyl-Asp-Glu-Val-Asp-CHO is compared with crystal structures of caspases-1 (2.3 A), -3 (2.2 A), and -8 (2.65 A) bound to the same inhibitor. Csp7 is a close homolog of caspase-3 (Csp3), and these two caspases possess some quarternary structural characteristics that support their unique role among the caspase family. However, although Csp3 and Csp7 are quite similar overall, they were found to have a significantly different substitution pattern of amino acids in and around the S4-binding site. CONCLUSIONS: These structures span all three caspase subgroups, and provide a basis for inferring substrate and inhibitor binding, as well as selectivity for the entire caspase family. This information will influence the design of selective caspase inhibitors to further elucidate the role of caspases in biology and hopefully lead to the design of therapeutic agents to treat caspase-mediated diseases, such as rheumatoid arthritis, certain neurogenerative diseases and stroke.
-==About this Structure==
-F1J is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. The following page contains interesting information on the relation of 1F1J with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb56_1.html Caspases]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1F1J OCA].
-==Reference==
-The structures of caspases-1, -3, -7 and -8 reveal the basis for substrate and inhibitor selectivity., Wei Y, Fox T, Chambers SP, Sintchak J, Coll JT, Golec JM, Swenson L, Wilson KP, Charifson PS, Chem Biol. 2000 Jun;7(6):423-32. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10873833 10873833]
 [[Category: Caspases]]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Charifson, P S.]]
+[[Category: RCSB PDB Molecule of the Month]]
-[[Category: Wei, Y.]]
+[[Category: Charifson PS]]
-[[Category: ACE]]
+[[Category: Wei Y]]
-[[Category: SO4]]
-[[Category: caspase-7]]
-[[Category: cysteine protease]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 11:03:08 2008''