4y11: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
==Trypsin in complex with with BPTI mutant (2S)-2-amino-4,4,4-trifluorobutanoic acid== | ==Trypsin in complex with with BPTI mutant (2S)-2-amino-4,4,4-trifluorobutanoic acid== | ||
<StructureSection load='4y11' size='340' side='right' caption='[[4y11]], [[Resolution|resolution]] 1.30Å' scene=''> | <StructureSection load='4y11' size='340' side='right' caption='[[4y11]], [[Resolution|resolution]] 1.30Å' scene=''> | ||
| Line 7: | Line 8: | ||
<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y0y|4y0y]], [[4y0z|4y0z]], [[4y10|4y10]]</td></tr> | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y0y|4y0y]], [[4y0z|4y0z]], [[4y10|4y10]]</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='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=4y11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y11 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4y11 RCSB], [http://www.ebi.ac.uk/pdbsum/4y11 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=4y11 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y11 OCA], [http://pdbe.org/4y11 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y11 RCSB], [http://www.ebi.ac.uk/pdbsum/4y11 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y11 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[http://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN]] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. | [[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®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4y11" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Basic Pancreatic Trypsin Inhibitor|Basic Pancreatic Trypsin Inhibitor]] | |||
*[[Trypsin|Trypsin]] | |||
== References == | |||
<references/> | |||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
Revision as of 09:14, 18 April 2018
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
Function[BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. Publication 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
|
| ||||||||||||||||||||||