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1pi2

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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pi2 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pi2 OCA], [http://www.ebi.ac.uk/pdbsum/1pi2 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pi2 RCSB]</span>
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[[Category: serine proteinase inhibitor]]
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Revision as of 20:00, 30 March 2008


PDB ID 1pi2

Drag the structure with the mouse to rotate
, resolution 2.5Å
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



REACTIVE SITES OF AN ANTICARCINOGENIC BOWMAN-BIRK PROTEINASE INHIBITOR ARE SIMILAR TO OTHER TRYPSIN INHIBITORS


Overview

The three-dimensional structure of the Bowman-Birk type proteinase inhibitor (PI-II) has been determined by x-ray crystallography and refined at 2.5-A resolution. This protein is a specific inhibitor of trypsin. Two reactive site loops, one at each end of the PI-II molecule, are structurally similar to each other and to reactive-site loops of pancreatic secretory trypsin inhibitor (Bolognesi, M., Gatti, G., Menegatti, E., Guarneri, M., Marquart, M., Papamokos, E., and Huber, R. (1982) J. Mol. Biol. 162, 839-869) and bovine pancreatic trypsin inhibitor (Deisenhofer, J., and Steigemann, W. (1975) Acta Crystallogr. B31, 238-250). PI-II is the first reported Bowman-Birk type inhibitor structure to be refined at high resolution, providing further insight into inhibitor mechanisms.

About this Structure

1PI2 is a Single protein structure of sequence from Glycine max. Full crystallographic information is available from OCA.

Reference

Reactive sites of an anticarcinogenic Bowman-Birk proteinase inhibitor are similar to other trypsin inhibitors., Chen P, Rose J, Love R, Wei CH, Wang BC, J Biol Chem. 1992 Jan 25;267(3):1990-4. PMID:1730730

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