5eg4: Difference between revisions

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-'''Unreleased structure'''
-The entry 5eg4 is ON HOLD
+==BOVINE TRYPSIN IN COMPLEX WITH CYCLIC INHIBITOR==
+<StructureSection load='5eg4' size='340' side='right'caption='[[5eg4]], [[Resolution|resolution]] 1.32&Aring;' scene=''>
+== Structural highlights ==
+<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='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.32&#8491;</td></tr>
+<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>
+</table>
+== Function ==
+[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN]
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+New 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.
-Authors: Knoerlein, A., Wagner, S., Heine, A., Steinmetzer, T., Klebe, G.
+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<ref>PMID:27280436</ref>
-Description: BOVINE TRYPSIN IN COMPLEX WITH CYCLIC INHIBITOR
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-[[Category: Unreleased Structures]]
+</div>
-[[Category: Steinmetzer, T]]
+<div class="pdbe-citations 5eg4" style="background-color:#fffaf0;"></div>
-[[Category: Klebe, G]]
-[[Category: Heine, A]]
+==See Also==
-[[Category: Knoerlein, A]]
+*[[Trypsin 3D structures|Trypsin 3D structures]]
-[[Category: Wagner, S]]
+== References ==
+<references/>
+__TOC__
+</StructureSection>
+[[Category: Bos taurus]]
+[[Category: Large Structures]]
+[[Category: Heine A]]
+[[Category: Klebe G]]
+[[Category: Knoerlein A]]
+[[Category: Steinmetzer T]]
+[[Category: Wagner S]]