2hex: Difference between revisions
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/he/2hex_consurf.spt"</scriptWhenChecked> | <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/he/2hex_consurf.spt"</scriptWhenChecked> | ||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
Latest revision as of 04:01, 21 November 2024
DECAMERS OBSERVED IN THE CRYSTALS OF BOVINE PANCREATIC TRYPSIN INHIBITORDECAMERS OBSERVED IN THE CRYSTALS OF BOVINE PANCREATIC TRYPSIN INHIBITOR
Structural highlights
FunctionBPT1_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 structure of bovine pancreatic trypsin inhibitor (BPTI) has been solved at 2.1 A resolution in a new crystal form (space group P6422 with unit-cell dimensions a = b = 95.0, c = 158.1 A). The asymmetric unit is a pentamer, but a decamer is created by application of crystallographic symmetry. The decamer of BPTI is only the fourth such assembly reported to date in the Protein Data Bank. Decamers observed in the crystals of bovine pancreatic trypsin inhibitor.,Lubkowski J, Wlodawer A Acta Crystallogr D Biol Crystallogr. 1999 Jan;55(Pt 1):335-7. Epub 1999, Jan 1. PMID:10089443[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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