View source for 8iyv


==Crystal structure of trypsin-famotidine complex at 2.10 Angstroms resolution==
<StructureSection load='8iyv' size='340' side='right'caption='[[8iyv]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[8iyv]] 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=8IYV OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=8IYV 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]] 2.1&#8491;</td></tr>
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene>, <scene name='pdbligand=FO9:3-[[2-[bis(azanyl)methylideneamino]-5~{H}-1,3-thiazol-4-yl]methylsulfanyl]-~{N}-sulfamoyl-propanimidamide'>FO9</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=8iyv FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=8iyv OCA], [https://pdbe.org/8iyv PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=8iyv RCSB], [https://www.ebi.ac.uk/pdbsum/8iyv PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=8iyv ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Serine proteases are among the important groups of enzymes having significant roles in cell biology. Trypsin is a representative member of the serine superfamily of enzymes, produced by acinar cells of pancreas. It is a validated drug target for various ailments including pancreatitis and colorectal cancer. Premature activation of trypsin is involved in the lysis of pancreatic tissues, which causes pancreatitis. It is also reported to be involved in colorectal carcinoma by activating other proteases, such as matrix metalloproteinase (MMPs). The development of novel trypsin inhibitors with good pharmacokinetic properties could play important roles in pharmaceutical sciences. This study reports the crystal structures of bovine pancreatic trypsin with four molecules; cimetidine, famotidine, pimagedine, and guanidine. These compounds possess binding affinity towards the active site (S1) of trypsin. The structures of all four complexes provided insight of the binding of four different ligands, as well as the dynamics of the active site towards the bind with different size ligands. This study might be helpful in designing of new potent inhibitors of trypsin and trypsin like serine proteases.

Structural basis for the binding of famotidine, cimetidine, guanidine, and pimagedine with serine protease.,Ahmad MS, Kalam N, Akbar Z, Shah N, Rasheed S, Choudhary MI Biochem Biophys Res Commun. 2024 Aug 24;733:150603. doi: , 10.1016/j.bbrc.2024.150603. PMID:39216203<ref>PMID:39216203</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 8iyv" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Large Structures]]
[[Category: Ahmad MS]]
[[Category: Akbar Z]]
[[Category: Choudhary MI]]
[[Category: Kalam N]]
[[Category: Rasheed S]]