5eg4: Difference between revisions
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<StructureSection load='5eg4' size='340' side='right'caption='[[5eg4]], [[Resolution|resolution]] 1.32Å' scene=''> | <StructureSection load='5eg4' size='340' side='right'caption='[[5eg4]], [[Resolution|resolution]] 1.32Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[5eg4]] is a 1 chain structure with sequence from [ | <table><tr><td colspan='2'>[[5eg4]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5EG4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5EG4 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.32Å</td></tr> | ||
<tr id=' | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</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=5eg4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5eg4 OCA], [https://pdbe.org/5eg4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5eg4 RCSB], [https://www.ebi.ac.uk/pdbsum/5eg4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5eg4 ProSAT]</span></td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | |||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Heine A]] | |||
[[Category: Heine | [[Category: Klebe G]] | ||
[[Category: Klebe | [[Category: Knoerlein A]] | ||
[[Category: Knoerlein | [[Category: Steinmetzer T]] | ||
[[Category: Steinmetzer | [[Category: Wagner S]] | ||
[[Category: Wagner | |||
Latest revision as of 07:01, 21 November 2024
BOVINE TRYPSIN IN COMPLEX WITH CYCLIC INHIBITORBOVINE TRYPSIN IN COMPLEX WITH CYCLIC INHIBITOR
Structural highlights
FunctionPublication Abstract from PubMedNew macrocyclic plasmin inhibitors based on our previously optimized P2-P3 core segment have been developed. In the first series, the P4 residue was modified, whereas the 4-amidinobenzylamide in P1 position was maintained. The originally used P4 benzylsulfonyl residue could be replaced by various sulfonyl- or urethane-like protecting groups. In the second series, the P1 benzamidine was modified and a strong potency and excellent selectivity was retained by incorporation of p-xylenediamine. Several analogues inhibit plasmin in the subnanomolar range, and their potency against related trypsin-like serine proteases including trypsin itself could be further reduced. Selected derivatives have been tested in a plasma fibrinolysis assay and are more effective than the reference inhibitor aprotinin. The crystal structure of one inhibitor was determined in complex with trypsin. The binding mode reveals a sterical clash of the inhibitor's linker segment with the 99-hairpin loop of trypsin, which is absent in plasmin. Optimization of Cyclic Plasmin Inhibitors: From Benzamidines to Benzylamines.,Hinkes S, Wuttke A, Saupe SM, Ivanova T, Wagner S, Knorlein A, Heine A, Klebe G, Steinmetzer T J Med Chem. 2016 Jun 17. PMID:27280436[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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