1ba7: Difference between revisions
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<StructureSection load='1ba7' size='340' side='right'caption='[[1ba7]], [[Resolution|resolution]] 2.50Å' scene=''> | <StructureSection load='1ba7' size='340' side='right'caption='[[1ba7]], [[Resolution|resolution]] 2.50Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ba7]] is a 2 chain structure with sequence from [ | <table><tr><td colspan='2'>[[1ba7]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BA7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BA7 FirstGlance]. <br> | ||
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | </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=1ba7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ba7 OCA], [https://pdbe.org/1ba7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ba7 RCSB], [https://www.ebi.ac.uk/pdbsum/1ba7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ba7 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
[[ | [[https://www.uniprot.org/uniprot/ITRA_SOYBN ITRA_SOYBN]] Inhibition of trypsin. | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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==See Also== | ==See Also== | ||
*[[Trypsin inhibitor|Trypsin inhibitor]] | *[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
Revision as of 19:08, 27 October 2021
SOYBEAN TRYPSIN INHIBITORSOYBEAN TRYPSIN INHIBITOR
Structural highlights
Function[ITRA_SOYBN] Inhibition of trypsin. 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 Kunitz-type soybean trypsin inhibitor (STI) has played a key role in the early study of proteinases, having been used as the main substrate in the biochemical and kinetic work that led to the definition of the standard mechanism of action of proteinase inhibitors. A partial structure of STI complexed with porcine trypsin has previously been reported, in which the first 93 residues of the inhibitor, including the region of contact with trypsin, were relatively well defined, whereas for the remaining part of the peptide chain only some Calpha atoms were located. The structure of the inhibitor in its free form has now been determined by molecular replacement to 2.5 A, using the coordinates of the homologous Erythrina trypsin inhibitor as a search model. When the refined atomic coordinates of STI are compared with the partial model previously available, the conformation of the reactive-site loop and its position with respect to the main body of the molecule does not change when the inhibitor interacts with trypsin. There are instead, despite the high similarity in the overall tertiary structure, significant differences between STI and Erythrina trypsin inhibitor (ETI) in the region which is in contact with the enzyme in the STI:trypsin crystal structure. Some of these differences can explain the unique specificity of ETI and its ability to inhibit the fibrinolytic enzyme tissue-type plasminogen activator. Structure of the Kunitz-type soybean trypsin inhibitor (STI): implication for the interactions between members of the STI family and tissue-plasminogen activator.,De Meester P, Brick P, Lloyd LF, Blow DM, Onesti S Acta Crystallogr D Biol Crystallogr. 1998 Jul 1;54(Pt 4):589-97. PMID:9761854[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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