View source for 5eg4


==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=5N7:(13S,16R)-N-(4-CARBAMIMIDOYLBENZYL)-16-((N-CYCLOHEXYLSULFAMOYL)AMINO)-3,9,15-TRIOXO-2,10,14-TRIAZA-6(1,4)-PIPERAZINA-1,11(1,4)-DIBENZENACYCLOHEPTADECAPHANE-13-CARBOXAMIDE'>5N7</scene>, <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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5eg4" style="background-color:#fffaf0;"></div>

==See Also==
*[[Trypsin 3D structures|Trypsin 3D structures]]
== 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]]