2xyh: Difference between revisions
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[[ | ==CASPASE-3:CAS60254719== | ||
<StructureSection load='2xyh' size='340' side='right' caption='[[2xyh]], [[Resolution|resolution]] 1.89Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[2xyh]] is a 2 chain structure 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=2XYH OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2XYH FirstGlance]. <br> | |||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=TQ9:5-CHLORO-4-OXOPENTANOIC+ACID'>TQ9</scene></td></tr> | |||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1nme|1nme]], [[1rhk|1rhk]], [[2j33|2j33]], [[1rhr|1rhr]], [[1nms|1nms]], [[1nmq|1nmq]], [[1rhq|1rhq]], [[1rhj|1rhj]], [[2cnn|2cnn]], [[2dko|2dko]], [[2c2k|2c2k]], [[2cjy|2cjy]], [[2j31|2j31]], [[2cnl|2cnl]], [[2c2m|2c2m]], [[2cnk|2cnk]], [[1cp3|1cp3]], [[2cjx|2cjx]], [[1re1|1re1]], [[2j30|2j30]], [[2xyg|2xyg]], [[2c1e|2c1e]], [[1pau|1pau]], [[2cdr|2cdr]], [[2j32|2j32]], [[1i3o|1i3o]], [[2cno|2cno]], [[1gfw|1gfw]], [[1rhu|1rhu]], [[1rhm|1rhm]], [[2c2o|2c2o]], [[1qx3|1qx3]]</td></tr> | |||
<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Caspase-3 Caspase-3], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.56 3.4.22.56] </span></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=2xyh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2xyh OCA], [http://www.rcsb.org/pdb/explore.do?structureId=2xyh RCSB], [http://www.ebi.ac.uk/pdbsum/2xyh PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Using a fragment-based docking procedure, several small-molecule inhibitors of caspase-3 were identified and tested and the crystal structures of three inhibitor complexes were determined. The crystal structures revealed that one inhibitor (NSC 18508) occupies only the S1 subsite, while two other inhibitors (NSC 89167 and NSC 251810) bind only to the prime part of the substrate-binding site. One of the major conformational changes observed in all three caspase-3-inhibitor complexes is a rotation of the Tyr204 side chain, which blocks the S2 subsite. In addition, the structural variability of the residues shaping the S1-S4 as well as the S1' subsites supports an induced-fit mechanism for the binding of the inhibitors in the active site. The high-resolution crystal structures reported here provide novel insights into the architecture of the substrate-binding site, which might be useful for the design of more potent caspase inhibitors. | |||
In silico identification and crystal structure validation of caspase-3 inhibitors without a P1 aspartic acid moiety.,Ganesan R, Jelakovic S, Mittl PR, Caflisch A, Grutter MG Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt, 8):842-50. Epub 2011 Jul 13. PMID:21821879<ref>PMID:21821879</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Caspase|Caspase]] | *[[Caspase|Caspase]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Caspase-3]] | [[Category: Caspase-3]] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
Revision as of 16:11, 22 October 2014
CASPASE-3:CAS60254719CASPASE-3:CAS60254719
Structural highlights
Publication Abstract from PubMedUsing a fragment-based docking procedure, several small-molecule inhibitors of caspase-3 were identified and tested and the crystal structures of three inhibitor complexes were determined. The crystal structures revealed that one inhibitor (NSC 18508) occupies only the S1 subsite, while two other inhibitors (NSC 89167 and NSC 251810) bind only to the prime part of the substrate-binding site. One of the major conformational changes observed in all three caspase-3-inhibitor complexes is a rotation of the Tyr204 side chain, which blocks the S2 subsite. In addition, the structural variability of the residues shaping the S1-S4 as well as the S1' subsites supports an induced-fit mechanism for the binding of the inhibitors in the active site. The high-resolution crystal structures reported here provide novel insights into the architecture of the substrate-binding site, which might be useful for the design of more potent caspase inhibitors. In silico identification and crystal structure validation of caspase-3 inhibitors without a P1 aspartic acid moiety.,Ganesan R, Jelakovic S, Mittl PR, Caflisch A, Grutter MG Acta Crystallogr Sect F Struct Biol Cryst Commun. 2011 Aug 1;67(Pt, 8):842-50. Epub 2011 Jul 13. PMID:21821879[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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