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1knt
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(New page: 200px<br /> <applet load="1knt" size="450" color="white" frame="true" align="right" spinBox="true" caption="1knt, resolution 1.6Å" /> '''THE 1.6 ANGSTROMS ST...)
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Revision as of 15:46, 12 November 2007
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THE 1.6 ANGSTROMS STRUCTURE OF THE KUNITZ-TYPE DOMAIN FROM THE ALPHA3 CHAIN OF THE HUMAN TYPE VI COLLAGEN
Contents |
Overview
The C-terminal Kunitz-type domain from the alpha 3 chain of human type VI, collagen (C5), a single 58 amino acid residue chain with three disulfide, bridges, was cloned, expressed and crystallized in a monoclonic form, space group P2(1), with a = 25.7 A, b = 38.2 A, c = 28.8 A and beta = 109, degrees. The structure was resolved by molecular replacement, using, Alzheimer's protein precursor inhibitor and bovine pancreatic trypsin, inhibitor three-dimensional structures as search models. The molecule with, one sulfate ion and 43 associated water molecules was refined by XPLOR to, an R-factor of 18.9% at 1.6 A. The molecule was not degraded by trypsin, and did not inhibit trypsin or tested serine proteases. As opposed to the, other Kunitz family members, C5 demonstrates left-handed chirality of the, Cys14-Cys38 disulfide bond. Inversion of the Thr13 carbonyl and bulky, side-chains at the interface with trypsin in a model of the C5-trypsin, complex may explain the lack of inhibition of trypsin.
Disease
Known diseases associated with this structure: Bethlem myopathy OMIM:[120250], Ullrich congenital muscular dystrophy OMIM:[120250]
About this Structure
1KNT is a Single protein structure of sequence from Homo sapiens with SO4 as ligand. Full crystallographic information is available from OCA.
Reference
The 1.6 A structure of Kunitz-type domain from the alpha 3 chain of human type VI collagen., Arnoux B, Merigeau K, Saludjian P, Norris F, Norris K, Bjorn S, Olsen O, Petersen L, Ducruix A, J Mol Biol. 1995 Mar 10;246(5):609-17. PMID:7533217
Page seeded by OCA on Mon Nov 12 17:52:49 2007
