5lgo

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m (Protected "5lgo" [edit=sysop:move=sysop])
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'''Unreleased structure'''
 
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The entry 5lgo is ON HOLD
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==Trypsin inhibitors for the treatment of pancreatitis - cpd 15==
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<StructureSection load='5lgo' size='340' side='right' caption='[[5lgo]], [[Resolution|resolution]] 1.12&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[5lgo]] is a 1 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=5LGO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5LGO FirstGlance]. <br>
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</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=6VZ:(2~{S},4~{S})-1-[4-(AMINOMETHYL)-3-METHOXY-PHENYL]CARBONYL-4-[4-(2-CYCLOPROPYLETHOXY)-6,8-DIHYDRO-5~{H}-PYRIDO[3,4-D]PYRIMIDIN-7-YL]-~{N}-METHYL-PYRROLIDINE-2-CARBOXAMIDE'>6VZ</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=DMS:DIMETHYL+SULFOXIDE'>DMS</scene></td></tr>
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<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[http://en.wikipedia.org/wiki/Trypsin Trypsin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.4 3.4.21.4] </span></td></tr>
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<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=5lgo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5lgo OCA], [http://pdbe.org/5lgo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5lgo RCSB], [http://www.ebi.ac.uk/pdbsum/5lgo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5lgo ProSAT]</span></td></tr>
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</table>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Proline-based trypsin inhibitors occupying the S1-S2-S1' region were identified by an HTS screening campaign. It was discovered that truncation of the P1' moiety and appropriate extension into the S4 region led to highly potent trypsin inhibitors with excellent selectivity against related serine proteases and a favorable hERG profile.
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Authors: Schiering, N., D'Arcy, A.
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Trypsin inhibitors for the treatment of pancreatitis.,Brandl T, Simic O, Skaanderup PR, Namoto K, Berst F, Ehrhardt C, Schiering N, Mueller I, Woelcke J Bioorg Med Chem Lett. 2016 Jul 17. pii: S0960-894X(16)30742-9. doi:, 10.1016/j.bmcl.2016.07.029. PMID:27476144<ref>PMID:27476144</ref>
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Description: Trypsin inhibitors for the treatment of pancreatitis -cpd 15
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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[[Category: Unreleased Structures]]
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</div>
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[[Category: D'Arcy, A]]
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<div class="pdbe-citations 5lgo" style="background-color:#fffaf0;"></div>
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== References ==
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<references/>
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__TOC__
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</StructureSection>
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[[Category: Bos taurus]]
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[[Category: Trypsin]]
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[[Category: Arcy, A D]]
[[Category: Schiering, N]]
[[Category: Schiering, N]]
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[[Category: Complex]]
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[[Category: Hydrolase]]
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[[Category: Inhibitor]]
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[[Category: Pancreatitis]]
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[[Category: S1 protease]]

Revision as of 16:11, 10 August 2016

Trypsin inhibitors for the treatment of pancreatitis - cpd 15

5lgo, resolution 1.12Å

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