4q2k: Difference between revisions
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''' | ==Bovine alpha chymotrypsin bound to a cyclic peptide inhibitor, 5b== | ||
<StructureSection load='4q2k' size='340' side='right' caption='[[4q2k]], [[Resolution|resolution]] 2.20Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4q2k]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Q2K OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Q2K FirstGlance]. <br> | |||
</td></tr><tr><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=5BF:(11S)-4,9-DIOXO-N-[(2S)-1-OXO-3-PHENYLPROPAN-2-YL]-17,22-DIOXA-10,30-DIAZATETRACYCLO[21.2.2.2~13,16~.1~5,8~]TRIACONTA-1(25),5,7,13,15,23,26,28-OCTAENE-11-CARBOXAMIDE'>5BF</scene><br> | |||
<tr><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Chymotrypsin Chymotrypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.1 3.4.21.1] </span></td></tr> | |||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4q2k FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4q2k OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4q2k RCSB], [http://www.ebi.ac.uk/pdbsum/4q2k PDBsum]</span></td></tr> | |||
<table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
There is a real need for simple structures that define a beta-strand conformation, a secondary structure that is central to peptide-protein interactions. For example, protease substrates and inhibitors almost universally adopt this geometry on active site binding. A planar pyrrole is used to replace two amino acids of a peptide backbone to generate a simple macrocycle that retains the required geometry for active site binding. The resulting beta-strand templates have reduced peptide character and provide potent protease inhibitors with the attachment of an appropriate amino aldehyde to the C-terminus. Picomolar inhibitors of cathepsin L and S are reported and the mode of binding of one example to the model protease chymotrypsin is defined by X-ray crystallography. | |||
Macrocyclic protease inhibitors with reduced Peptide character.,Chua KC, Pietsch M, Zhang X, Hautmann S, Chan HY, Bruning JB, Gutschow M, Abell AD Angew Chem Int Ed Engl. 2014 Jul 21;53(30):7828-31. doi: 10.1002/anie.201404301. , Epub 2014 Jun 5. PMID:24903745<ref>PMID:24903745</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Bos taurus]] | |||
[[Category: Chymotrypsin]] | |||
[[Category: Abell, A D.]] | |||
[[Category: Bruning, J B.]] | |||
[[Category: Chan, H Y.]] | |||
[[Category: Chymotrypsin]] | |||
[[Category: Hydrolase-hydrolase inhibitor complex]] | |||
[[Category: Protease]] | |||
Revision as of 08:01, 23 July 2014
Bovine alpha chymotrypsin bound to a cyclic peptide inhibitor, 5b
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