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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'''THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR IN SOLUTION'''<br />
'''THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR IN SOLUTION'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1BBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BBI OCA].
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1BBI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of 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=1BBI OCA].
==Reference==
==Reference==
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[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Wemmer, D.E.]]
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[[Category: Wemmer, D E.]]
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[[Category: Werner, M.H.]]
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[[Category: Werner, M H.]]
[[Category: serine protease inhibitor]]
[[Category: serine protease inhibitor]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:31:29 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:53:31 2008''

Revision as of 09:53, 21 February 2008


1bbi

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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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