2bbi: Difference between revisions

Revision as of 17:36, 21 February 2008

THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR IN SOLUTION

OverviewOverview

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 StructureAbout this Structure

2BBI is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

ReferenceReference

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

Page seeded by OCA on Thu Feb 21 16:36:03 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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-[[Image:2bbi.jpg|left|200px]]<br /><applet load="2bbi" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:2bbi.jpg|left|200px]]<br /><applet load="2bbi" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="2bbi" />
 '''THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR IN SOLUTION'''<br />
 ==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.
+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==
-BBI 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=2BBI OCA].
+BBI 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=2BBI OCA].
 ==Reference==
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 [[Category: Glycine max]]
 [[Category: Single protein]]
-[[Category: Wemmer, D.E.]]
+[[Category: Wemmer, D E.]]
-[[Category: Werner, M.H.]]
+[[Category: Werner, M H.]]
 [[Category: serine protease inhibitor]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 08:42:00 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:36:03 2008''