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| | <StructureSection load='4y0z' size='340' side='right'caption='[[4y0z]], [[Resolution|resolution]] 1.37Å' scene=''> | | <StructureSection load='4y0z' size='340' side='right'caption='[[4y0z]], [[Resolution|resolution]] 1.37Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[4y0z]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4Y0Z OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4Y0Z FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[4y0z]] 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=4Y0Z OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4Y0Z FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</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='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=ABA:ALPHA-AMINOBUTYRIC+ACID'>ABA</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=4y0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0z OCA], [https://pdbe.org/4y0z PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4y0z RCSB], [https://www.ebi.ac.uk/pdbsum/4y0z PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0z ProSAT]</span></td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[4y0y|4y0y]], [[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=4y0z FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4y0z OCA], [http://pdbe.org/4y0z PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4y0z RCSB], [http://www.ebi.ac.uk/pdbsum/4y0z PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4y0z ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN]] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. | + | [https://www.uniprot.org/uniprot/TRY1_BOVIN TRY1_BOVIN] |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | ==See Also== | | ==See Also== |
| | *[[BPTI 3D structures|BPTI 3D structures]] | | *[[BPTI 3D structures|BPTI 3D structures]] |
| - | *[[Trypsin|Trypsin]] | + | *[[Trypsin 3D structures|Trypsin 3D structures]] |
| | == References == | | == References == |
| | <references/> | | <references/> |
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| | [[Category: Bos taurus]] | | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Trypsin]]
| + | [[Category: Alings C]] |
| - | [[Category: Alings, C]] | + | [[Category: Berger AA]] |
| - | [[Category: Berger, A A]] | + | [[Category: Koksch B]] |
| - | [[Category: Koksch, B]] | + | [[Category: Loll B]] |
| - | [[Category: Loll, B]] | + | [[Category: Muelow U]] |
| - | [[Category: Muelow, U]] | + | [[Category: Wahl MC]] |
| - | [[Category: Wahl, M C]] | + | [[Category: Ye S]] |
| - | [[Category: Ye, S]] | + | |
| - | [[Category: Hydrolase inhibitor]]
| + | |
| - | [[Category: Hydrolase-hydrolase inhibitor complex]]
| + | |
| - | [[Category: Hydrolase-hydrolase inhibitor complex complex]]
| + | |
| - | [[Category: Metal-binding]]
| + | |
| - | [[Category: Serine protease]]
| + | |
| Structural highlights
Function
TRY1_BOVIN
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[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Ye S, Loll B, Berger AA, Mulow U, Alings C, Wahl MC, Koksch B. Fluorine teams up with water to restore inhibitor activity to mutant BPTI. Chem Sci. 2015 Sep 1;6(9):5246-5254. doi: 10.1039/c4sc03227f. Epub 2015 Jun 12. PMID:29449928 doi:http://dx.doi.org/10.1039/c4sc03227f
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