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[[Image:1oa5.jpg|left|200px]]
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{{STRUCTURE_1oa5|  PDB=1oa5  |  SCENE=  }}
'''THE SOLUTION STRUCTURE OF BOVINE PANCREATIC TRYPSIN INHIBITOR AT HIGH PRESSURE'''


==The solution structure of bovine pancreatic trypsin inhibitor at high pressure==
<StructureSection load='1oa5' size='340' side='right'caption='[[1oa5]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1oa5]] is a 1 chain structure with sequence from [https://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 [https://proteopedia.org/fgij/fg.htm?mol=1OA5 FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 3 models</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=1oa5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1oa5 OCA], [https://pdbe.org/1oa5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1oa5 RCSB], [https://www.ebi.ac.uk/pdbsum/1oa5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1oa5 ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/BPT1_BOVIN BPT1_BOVIN] Inhibits trypsin, kallikrein, chymotrypsin, and plasmin.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <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/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1oa5 ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The 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.


==Overview==
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<ref>PMID:12930996</ref>
The 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.


==About this Structure==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
1OA5 is a [[Single protein]] structure of 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=1OA5 OCA].
</div>
<div class="pdbe-citations 1oa5" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/12930996 12930996]
*[[BPTI 3D structures|BPTI 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Akasaka, K.]]
[[Category: Akasaka K]]
[[Category: Refaee, M.]]
[[Category: Refaee M]]
[[Category: Williamson, M P.]]
[[Category: Williamson MP]]
[[Category: Protease inhibitor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 03:35:05 2008''

Latest revision as of 07:32, 23 October 2024

The solution structure of bovine pancreatic trypsin inhibitor at high pressure

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