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| | <StructureSection load='5jb5' size='340' side='right'caption='[[5jb5]], [[Resolution|resolution]] 1.60Å' scene=''> | | <StructureSection load='5jb5' size='340' side='right'caption='[[5jb5]], [[Resolution|resolution]] 1.60Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[5jb5]] is a 3 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5JB5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5JB5 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[5jb5]] is a 3 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=5JB5 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5JB5 FirstGlance]. <br> |
| - | </td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><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]] 1.6Å</td></tr> |
| - | <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[5jb4|5jb4]], [[5jb6|5jb6]], [[5jb7|5jb7]]</td></tr> | + | <tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=5jb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jb5 OCA], [http://pdbe.org/5jb5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=5jb5 RCSB], [http://www.ebi.ac.uk/pdbsum/5jb5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=5jb5 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=5jb5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5jb5 OCA], [https://pdbe.org/5jb5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5jb5 RCSB], [https://www.ebi.ac.uk/pdbsum/5jb5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5jb5 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/BPT1_BOVIN BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. |
| | <div style="background-color:#fffaf0;"> | | <div style="background-color:#fffaf0;"> |
| | == Publication Abstract from PubMed == | | == Publication Abstract from PubMed == |
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| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Bovin]] | + | [[Category: Bos taurus]] |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Islam, M M]] | + | [[Category: Islam MM]] |
| - | [[Category: Hydrolase inhibitor]]
| + | |
| - | [[Category: Proteinase inhibitor]]
| + | |
| Structural highlights
Function
BPT1_BOVIN Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
Publication Abstract from PubMed
We report a thermodynamic and structural analysis of six extensively simplified bovine pancreatic trypsin inhibitor (BPTI) variants containing 19-24 alanines out of 58 residues. Differential scanning calorimetry indicated a two-state thermal unfolding, typical of a native protein with densely packed interior. Surprisingly, increasing the number of alanines induced enthalpy stabilization, which was however over-compensated by entropy destabilization. X-ray crystallography indicated that the alanine substitutions caused the recruitment of novel water molecules facilitating the formation of protein-water hydrogen bonds and improving the hydration shells around the alanine's methyl groups, both of which presumably contributed to enthalpy stabilization. There was a strong correlation between the number of water molecules and the thermodynamic parameters. Overall, our results demonstrate that, in contrast to our initial expectation, a protein sequence in which over 40% of the residues are alanines can retain a densely packed structure and undergo thermal denaturation with a large enthalpy change, mainly contributed by hydration.
Crystal structures of highly simplified BPTIs provide insights into hydration-driven increase of unfolding enthalpy.,Islam MM, Yohda M, Kidokoro SI, Kuroda Y Sci Rep. 2017 Mar 7;7:41205. doi: 10.1038/srep41205. PMID:28266637[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
See Also
References
- ↑ Islam MM, Yohda M, Kidokoro SI, Kuroda Y. Crystal structures of highly simplified BPTIs provide insights into hydration-driven increase of unfolding enthalpy. Sci Rep. 2017 Mar 7;7:41205. doi: 10.1038/srep41205. PMID:28266637 doi:http://dx.doi.org/10.1038/srep41205
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