1bbi
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(New page: 200px<br /><applet load="1bbi" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bbi" /> '''THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPS...)
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Revision as of 09:24, 20 November 2007
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THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR IN SOLUTION
Overview
The three-dimensional structure of soybean trypsin/chymotrypsin, Bowman-Birk inhibitor in solution has been determined by two-dimensional, 1H nuclear magnetic resonance spectroscopy and dynamical simulated, annealing using the program XPLOR. The structure was defined by 907 NOEs, involving intra- and interresidue contacts which served as distance, constraints for a protocol of dynamical simulated annealing. In addition, 48 phi angle constraints involving non-proline amino acids, 29 chi angle, constraints, six omega angle constraints for the X-Pro peptide bond, and, 35 stereoassignments for prochiral centers were incorporated during the, course of the calculation. The protein is characterized by two distinct, binding domains for serine protease. Each domain is comprised of a, beta-hairpin (antiparallel beta-sheet and a cis-proline-containing type, VIb reverse turn) with a short segment making a third strand of, antiparallel beta-sheet. The structure determination and refinement are, described, and the structure is compared to other structures of, Bowman-Birk inhibitors as well as other families of serine protease, inhibitors.
About this Structure
1BBI is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.
Reference
Three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution., Werner MH, Wemmer DE, Biochemistry. 1992 Feb 4;31(4):999-1010. PMID:1734975
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