1oa5: Difference between revisions
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== | |||
==The solution structure of bovine pancreatic trypsin inhibitor at high pressure== | |||
<StructureSection load='1oa5' size='340' side='right' caption='[[1oa5]], [[NMR_Ensembles_of_Models | 3 NMR models]]' scene=''> | <StructureSection load='1oa5' size='340' side='right' caption='[[1oa5]], [[NMR_Ensembles_of_Models | 3 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1oa5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OA5 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1oa5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OA5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1OA5 FirstGlance]. <br> | ||
</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aal|1aal]], [[1b0c|1b0c]], [[1bhc|1bhc]], [[1bpi|1bpi]], [[1bpt|1bpt]], [[1bth|1bth]], [[1bti|1bti]], [[1bz5|1bz5]], [[1bzx|1bzx]], [[1cbw|1cbw]], [[1d0d|1d0d]], [[1eaw|1eaw]], [[1ejm|1ejm]], [[1f5r|1f5r]], [[1f7z|1f7z]], [[1fan|1fan]], [[1fy8|1fy8]], [[1g6x|1g6x]], [[1jv8|1jv8]], [[1jv9|1jv9]], [[1k6u|1k6u]], [[1ld5|1ld5]], [[1ld6|1ld6]], [[1mtn|1mtn]], [[1nag|1nag]], [[1oa6|1oa6]], [[1pit|1pit]], [[1qlq|1qlq]], [[1tpa|1tpa]], [[2hex|2hex]], [[2kai|2kai]], [[2ptc|2ptc]], [[2tgp|2tgp]], [[2tpi|2tpi]], [[3btd|3btd]], [[3bte|3bte]], [[3btf|3btf]], [[3btg|3btg]], [[3bth|3bth]], [[3btk|3btk]], [[3btm|3btm]], [[3btq|3btq]], [[3btt|3btt]], [[3btw|3btw]], [[3tgi|3tgi]], [[3tgj|3tgj]], [[3tgk|3tgk]], [[3tpi|3tpi]], [[4pti|4pti]], [[4tpi|4tpi]], [[5pti|5pti]], [[6pti|6pti]], [[7pti|7pti]], [[8pti|8pti]], [[9pti|9pti]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1aal|1aal]], [[1b0c|1b0c]], [[1bhc|1bhc]], [[1bpi|1bpi]], [[1bpt|1bpt]], [[1bth|1bth]], [[1bti|1bti]], [[1bz5|1bz5]], [[1bzx|1bzx]], [[1cbw|1cbw]], [[1d0d|1d0d]], [[1eaw|1eaw]], [[1ejm|1ejm]], [[1f5r|1f5r]], [[1f7z|1f7z]], [[1fan|1fan]], [[1fy8|1fy8]], [[1g6x|1g6x]], [[1jv8|1jv8]], [[1jv9|1jv9]], [[1k6u|1k6u]], [[1ld5|1ld5]], [[1ld6|1ld6]], [[1mtn|1mtn]], [[1nag|1nag]], [[1oa6|1oa6]], [[1pit|1pit]], [[1qlq|1qlq]], [[1tpa|1tpa]], [[2hex|2hex]], [[2kai|2kai]], [[2ptc|2ptc]], [[2tgp|2tgp]], [[2tpi|2tpi]], [[3btd|3btd]], [[3bte|3bte]], [[3btf|3btf]], [[3btg|3btg]], [[3bth|3bth]], [[3btk|3btk]], [[3btm|3btm]], [[3btq|3btq]], [[3btt|3btt]], [[3btw|3btw]], [[3tgi|3tgi]], [[3tgj|3tgj]], [[3tgk|3tgk]], [[3tpi|3tpi]], [[4pti|4pti]], [[4tpi|4tpi]], [[5pti|5pti]], [[6pti|6pti]], [[7pti|7pti]], [[8pti|8pti]], [[9pti|9pti]]</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=1oa5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oa5 OCA], [http://pdbe.org/1oa5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oa5 RCSB], [http://www.ebi.ac.uk/pdbsum/1oa5 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=1oa5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oa5 OCA], [http://pdbe.org/1oa5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1oa5 RCSB], [http://www.ebi.ac.uk/pdbsum/1oa5 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1oa5 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oa5_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/oa/1oa5_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
| Line 27: | Line 28: | ||
</div> | </div> | ||
<div class="pdbe-citations 1oa5" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 1oa5" style="background-color:#fffaf0;"></div> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 10:29, 7 February 2018
The solution structure of bovine pancreatic trypsin inhibitor at high pressureThe solution structure of bovine pancreatic trypsin inhibitor at high pressure
Structural highlights
Function[BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedThe solution structure of bovine pancreatic trypsin inhibitor (BPTI) at a pressure of 2 kbar is presented. The structure was calculated as a change from an energy-minimized low-pressure structure, using (1)H chemical shifts as restraints. The structure has changed by 0.24 A RMS, and has almost unchanged volume. The largest changes as a result of pressure are in the loop 10-16, which contains the active site of BPTI, and residues 38-42, which are adjacent to buried water molecules. Hydrogen bonds are compressed by 0.029 +/- 0.117 A, with the longer hydrogen bonds, including those to internal buried water molecules, being compressed more. The hydrophobic core is also compressed, largely from reduction of packing defects. The parts of the structure that have the greatest change are close to buried water molecules, thus highlighting the importance of water molecules as the nucleation sites for volume fluctuation of proteins in native conditions. The solution structure of bovine pancreatic trypsin inhibitor at high pressure.,Williamson MP, Akasaka K, Refaee M Protein Sci. 2003 Sep;12(9):1971-9. PMID:12930996[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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