1gl1 | pdb_00001gl1

STRUCTURE OF THE COMPLEX BETWEEN BOVINE ALPHA-CHYMOTRYPSIN AND PMP-C, AN INHIBITOR FROM THE INSECT LOCUSTA MIGRATORIA

spinqualitylabelsall models 1gl1, resolution 2.10Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 1gl1 is a 6 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance. Ligands: CD Related: 1ab9, 1acb, 1afq, 1ca0, 1cbw, 1cgi, 1cgj, 1chg, 1dlk, 1ex3, 1gcd, 1gct, 1gg6, 1ggd, 1gha, 1ghb, 1gl0, 1gmc, 1gmd, 1gmh, 1hja, 1mtn, 1pmc, 1vgc, 2cga, 2gch, 2gct, 2gmt, 2vgc, 3gch, 3gct, 3vgc, 4gch, 4vgc, 5gch, 6gch, 7gch, 8gch Activity: Chymotrypsin, with EC number 3.4.21.1 Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [LCM_LOCMI] Both LCMI I and II are inhibitors of chymotrypsin and elastase (in vitro). They both inhibit the prophenol oxidase activation cascade. 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 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). 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 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See Also Chymotrypsin

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