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'''STRUCTURE OF THE COMPLEX BETWEEN BOVINE ALPHA-CHYMOTRYPSIN AND PMP-C, AN INHIBITOR FROM THE INSECT LOCUSTA MIGRATORIA''' | '''STRUCTURE OF THE COMPLEX BETWEEN BOVINE ALPHA-CHYMOTRYPSIN AND PMP-C, AN INHIBITOR FROM THE INSECT LOCUSTA MIGRATORIA''' | ||
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[[Category: Kellenberger, C.]] | [[Category: Kellenberger, C.]] | ||
[[Category: Roussel, A.]] | [[Category: Roussel, A.]] | ||
[[Category: | [[Category: Hydrolase]] | ||
[[Category: | [[Category: Serine protease]] | ||
[[Category: | [[Category: Serine protease inhibitor]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:42:40 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 17:42, 2 May 2008
STRUCTURE OF THE COMPLEX BETWEEN BOVINE ALPHA-CHYMOTRYPSIN AND PMP-C, AN INHIBITOR FROM THE INSECT LOCUSTA MIGRATORIA
OverviewOverview
The crystal structures of two homologous inhibitors (PMP-C and PMP-D2v) from the insect Locusta migratoria have been determined in complex with bovine alpha-chymotrypsin at 2.1- and 3.0-A resolution, respectively. PMP-C is a potent bovine alpha-chymotrypsin inhibitor whereas native PMP-D2 is a weak inhibitor of bovine trypsin. One unique mutation at the P1 position converts PMP-D2 into a potent bovine alpha-chymotrypsin inhibitor. The two peptides have a similar overall conformation, which consists of a triple-stranded antiparallel beta-sheet connected by three disulfide bridges, thus defining a novel family of serine protease inhibitors. They have in common the protease interaction site, which is composed of the classical protease binding loop (position P5 to P'4, corresponding to residues 26-34) and of an internal segment (residues 15-18), held together by two disulfide bridges. Structural divergences between the two inhibitors result in an additional interaction site between PMP-D2v (position P10 to P6, residues 21-25) and the residues 172-175 of alpha-chymotrypsin. This unusual interaction may be responsible for species selectivity. A careful comparison of data on bound and free inhibitors (from this study and previous NMR studies, respectively) suggests that complexation to the protease stabilizes the flexible binding loop (from P5 to P'4).
About this StructureAbout this Structure
1GL1 is a Protein complex structure of sequences from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Complexation of two proteic insect inhibitors to the active site of chymotrypsin suggests decoupled roles for binding and selectivity., Roussel A, Mathieu M, Dobbs A, Luu B, Cambillau C, Kellenberger C, J Biol Chem. 2001 Oct 19;276(42):38893-8. Epub 2001 Aug 8. PMID:11495915 Page seeded by OCA on Fri May 2 17:42:40 2008