1k9b: Difference between revisions

Revision as of 09:59, 2 July 2008

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File:1k9b.png

Template:STRUCTURE 1k9b

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

Template:ABSTRACT PUBMED 8954162

About this StructureAbout this Structure

1K9B is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

ReferenceReference

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

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-'''Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation'''
+===Crystal structure of the bifunctional soybean Bowman-Birk inhibitor at 0.28 nm resolution. Structural peculiarities in a folded protein conformation===
-==Overview==
+<!--
-The 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. &amp; 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--&gt;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.
+The line below this paragraph, {{ABSTRACT_PUBMED_8954162}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_8954162}}
 ==About this Structure==
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 [[Category: Double-headed]]
 [[Category: Tripple-stranded beta hairpin]]
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