4y11: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[4y11]] is a 2 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=4Y11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y11 FirstGlance]. <br> | <table><tr><td colspan='2'>[[4y11]] is a 2 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=4Y11 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y11 FirstGlance]. <br> | ||
</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3EG:(2S)-2-AMINO-4,4,4-TRIFLUOROBUTANOIC+ACID'>3EG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr> | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.3Å</td></tr> | ||
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=3EG:(2S)-2-AMINO-4,4,4-TRIFLUOROBUTANOIC+ACID'>3EG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GOL:GLYCEROL'>GOL</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=4y11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y11 OCA], [https://pdbe.org/4y11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y11 RCSB], [https://www.ebi.ac.uk/pdbsum/4y11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y11 ProSAT]</span></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=4y11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y11 OCA], [https://pdbe.org/4y11 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y11 RCSB], [https://www.ebi.ac.uk/pdbsum/4y11 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y11 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
Latest revision as of 06:42, 21 November 2024
Trypsin in complex with with BPTI mutant (2S)-2-amino-4,4,4-trifluorobutanoic acidTrypsin in complex with with BPTI mutant (2S)-2-amino-4,4,4-trifluorobutanoic acid
Structural highlights
FunctionPublication Abstract from PubMedIntroducing 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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