1k9b: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1k9b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K9B FirstGlance]. <br> | <table><tr><td colspan='2'>[[1k9b]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1K9B OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1K9B FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d6r|1d6r]], [[1bbi|1bbi]], [[1pbi|1pbi]], [[1c2a|1c2a]], [[1pi2|1pi2]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1d6r|1d6r]], [[1bbi|1bbi]], [[1pbi|1pbi]], [[1c2a|1c2a]], [[1pi2|1pi2]]</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1k9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k9b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k9b RCSB], [http://www.ebi.ac.uk/pdbsum/1k9b 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=1k9b FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1k9b OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1k9b RCSB], [http://www.ebi.ac.uk/pdbsum/1k9b PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://www.uniprot.org/uniprot/IBB1_SOYBN IBB1_SOYBN]] Inhibitor of trypsin and of chymotrypsin. | |||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Glycine max]] | [[Category: Glycine max]] | ||
[[Category: Ermler, U | [[Category: Ermler, U]] | ||
[[Category: Essen, L O | [[Category: Essen, L O]] | ||
[[Category: Flecker, P | [[Category: Flecker, P]] | ||
[[Category: Kim, Y M | [[Category: Kim, Y M]] | ||
[[Category: Voss, R H | [[Category: Voss, R H]] | ||
[[Category: Wenzl, G | [[Category: Wenzl, G]] | ||
[[Category: Double-headed]] | [[Category: Double-headed]] | ||
[[Category: Hydrolase inhibitor]] | [[Category: Hydrolase inhibitor]] | ||
[[Category: Tripple-stranded beta hairpin]] | [[Category: Tripple-stranded beta hairpin]] | ||
Revision as of 06:44, 25 December 2014
Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformationCrystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation
Structural highlights
Function[IBB1_SOYBN] Inhibitor of trypsin and of chymotrypsin. 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 Bowman-Birk inhibitor from soybean is a small protein that contains a binary arrangement of trypsin-reactive and chymotrypsin-reactive subdomains. In this report, the crystal structure of this anticarcinogenic protein has been determined to 0.28-nm resolution by molecular replacement from crystals grown at neutral pH. The crystal structure differs from a previously determined NMR structure [Werner, M. H. & Wemmer, D. E. (1992) Biochemistry 31, 999-1010] in the relative orientation of the two enzyme-insertion loops, in some details of the main chain trace, in the presence of favourable contacts in the trypsin-insertion loop, and in the orientation of several amino acid side chains. The proximity of Met27 and Gln48 in the X-ray structure contradicts the solution structure, in which these two side chains point away from each other. The significant effect of a Met27-->Ile replacement on the inhibitory activity of the chymotrypsin-reactive subdomain agrees with the X-ray structure. Exposed hydrophobic patches, the presence of charged amino acid residues, and the presence of water molecules in the protein interior are in contrast to standard proteins that comprise a hydrophobic core and exposed polar amino acids. Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28-nm resolution. Structural peculiarities in a folded protein conformation.,Voss RH, Ermler U, Essen LO, Wenzl G, Kim YM, Flecker P Eur J Biochem. 1996 Nov 15;242(1):122-31. PMID:8954162[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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