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[[Image:2bbi.jpg|left|200px]]
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{{STRUCTURE_2bbi|  PDB=2bbi  |  SCENE=  }}
'''THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR IN SOLUTION'''


==THREE-DIMENSIONAL STRUCTURE OF SOYBEAN TRYPSIN(SLASH)CHYMOTRYPSIN BOWMAN-BIRK INHIBITOR IN SOLUTION==
<StructureSection load='2bbi' size='340' side='right'caption='[[2bbi]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2bbi]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Glycine_max Glycine max]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2BBI OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2BBI FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 16 models</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2bbi FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2bbi OCA], [https://pdbe.org/2bbi PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2bbi RCSB], [https://www.ebi.ac.uk/pdbsum/2bbi PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2bbi ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/IBB1_SOYBN IBB1_SOYBN] Inhibitor of trypsin and of chymotrypsin.
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
  <jmolCheckbox>
    <scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/bb/2bbi_consurf.spt"</scriptWhenChecked>
    <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked>
    <text>to colour the structure by Evolutionary Conservation</text>
  </jmolCheckbox>
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=2bbi ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
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.


==Overview==
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<ref>PMID:1734975</ref>
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==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
2BBI is a [[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].
</div>
<div class="pdbe-citations 2bbi" style="background-color:#fffaf0;"></div>


==Reference==
==See Also==
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:[http://www.ncbi.nlm.nih.gov/pubmed/1734975 1734975]
*[[Trypsin inhibitor 3D structures|Trypsin inhibitor 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Glycine max]]
[[Category: Glycine max]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Wemmer, D E.]]
[[Category: Wemmer DE]]
[[Category: Werner, M H.]]
[[Category: Werner MH]]
[[Category: Serine protease inhibitor]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 20:04:23 2008''

Latest revision as of 10:46, 23 October 2024

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

Structural highlights

2bbi is a 1 chain structure with sequence from Glycine max. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:Solution NMR, 16 models
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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 PubMed

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

  1. ↑ Werner MH, Wemmer DE. Three-dimensional structure of soybean trypsin/chymotrypsin Bowman-Birk inhibitor in solution. Biochemistry. 1992 Feb 4;31(4):999-1010. PMID:1734975
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