1pbi: Difference between revisions

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[[Image:1pbi.jpg|left|200px]]
{{Seed}}
[[Image:1pbi.png|left|200px]]


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{{STRUCTURE_1pbi|  PDB=1pbi  |  SCENE=  }}  
{{STRUCTURE_1pbi|  PDB=1pbi  |  SCENE=  }}  


'''CRYSTAL STRUCTURE OF A BOWMAN-BIRK INHIBITOR FROM PEA SEEDS'''
===CRYSTAL STRUCTURE OF A BOWMAN-BIRK INHIBITOR FROM PEA SEEDS===




==Overview==
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The trypsin/chymotrypsin inhibitors from winter pea seeds (PsTI) are members of the Bowman-Birk protease inhibitor (BBPI) family. The crystal structure of the isoform PsTI-IVb was determined by molecular replacement at 2.7 A resolution using the X-ray co-ordinates of the soybean inhibitor as a search model. The inhibitor crystallized with a nearly perfect 2-fold symmetric dimer in the asymmetric unit. Although the overall structure is very similar to that seen in other BBPIs, there are notable new structural features. Unlike the previously reported X-ray structures of BBPIs, the structure of PsTI-IVb includes the C-terminal segment of the molecule. The C-terminal tail of each subunit is partly beta-stranded and interacts with the 2-fold symmetry-related subunit, forming a beta-sheet with strands A and B of this subunit. The dimer is mainly stabilized by a large internal hydrogen-bonded network surrounded by two hydrophobic links. Fluorescence anisotropy decay measurements show that residues Tyr59 and Tyr43 are mobile in the picosecond time scale with a large amplitude. The fluorescence study and a molecular model of the simultaneous binding of PsTI-IVb to porcine trypsin and bovine chymotrypsin are compatible only with a monomeric state of the functional molecule in solution.
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{{ABSTRACT_PUBMED_9887273}}


==About this Structure==
==About this Structure==
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[[Category: Chymotrypsin inhibitor]]
[[Category: Chymotrypsin inhibitor]]
[[Category: Trypsin inhibitor]]
[[Category: Trypsin inhibitor]]
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