4y0y: Difference between revisions

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 ==Trypsin in complex with with BPTI==
 <StructureSection load='4y0y' size='340' side='right' caption='[[4y0y]], [[Resolution|resolution]] 1.25&Aring;' scene=''>
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 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y0z|4y0z]], [[4y10|4y10]], [[4y11|4y11]]</td></tr>
 <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>
-<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=4y0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0y OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y0y RCSB], [http://www.ebi.ac.uk/pdbsum/4y0y PDBsum]</span></td></tr>
+<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=4y0y FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0y OCA], [http://pdbe.org/4y0y PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y0y RCSB], [http://www.ebi.ac.uk/pdbsum/4y0y PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0y ProSAT]</span></td></tr>
 </table>
 == Function ==
 [[http://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN]] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
+<div style="background-color:#fffaf0;">
+== Publication Abstract from PubMed ==
+Introducing fluorine into molecules has a wide range of effects on their physicochemical properties, often desirable but in most cases unpredictable. The fluorine atom imparts the C-F bond with low polarizability and high polarity, and significantly affects the behavior of neighboring functional groups, in a covalent or noncovalent manner. Here, we report that fluorine, present in the form of a single fluoroalkyl amino acid side chain in the P1 position of the well-characterized serine-protease inhibitor BPTI, can fully restore inhibitor activity to a mutant that contains the corresponding hydrocarbon side chain at the same site. High resolution crystal structures were obtained for four BPTI variants in complex with bovine beta-trypsin, revealing changes in the stoichiometry and dynamics of water molecules in the S1 subsite. These results demonstrate that the introduction of fluorine into a protein environment can result in "chemical complementation" that has a significantly favorable impact on protein-protein interactions.
+Fluorine teams up with water to restore inhibitor activity to mutant BPTI.,Ye S, Loll B, Berger AA, Mulow U, Alings C, Wahl MC, Koksch B Chem Sci. 2015 Sep 1;6(9):5246-5254. doi: 10.1039/c4sc03227f. Epub 2015 Jun 12. PMID:29449928<ref>PMID:29449928</ref>
+From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
+</div>
+<div class="pdbe-citations 4y0y" style="background-color:#fffaf0;"></div>
+==See Also==
+*[[Basic Pancreatic Trypsin Inhibitor|Basic Pancreatic Trypsin Inhibitor]]
+*[[Trypsin|Trypsin]]
+== References ==
+<references/>
 __TOC__
 </StructureSection>