1pcp
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(New page: 200px<br /><applet load="1pcp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pcp" /> '''SOLUTION STRUCTURE OF A TREFOIL-MOTIF-CONTAI...)
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Revision as of 21:34, 20 November 2007
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SOLUTION STRUCTURE OF A TREFOIL-MOTIF-CONTAINING CELL GROWTH FACTOR, PORCINE SPASMOLYTIC PROTEIN
Overview
The porcine spasmolytic protein (pSP) is a 106-residue cell growth factor, that typifies a family of eukaryotic proteins that contain at least one, copy of an approximately 40-amino acid protein domain known as the trefoil, motif. In fact, pSP contains two highly homologous trefoil domains. We, have determined the complete three-dimensional solution structure of pSP, by using a combination of two- and three-dimensional 1H NMR spectroscopy, and distance geometry calculations. pSP is a relatively elongated, molecule, consisting of two compact globular domains joined via a small, interface. The protein's two trefoil domains adopt the same tertiary, structure and contain a core C-terminal two-stranded antiparallel, beta-sheet, preceded by a 6-residue helix that packs against the, N-terminal beta-strand. The remainder of the protein backbone is taken up, by two short loops that lie on either side of the beta-hairpin and are, linked by an extended region that wraps around the C-terminal beta-strand., The topology of the protein backbone observed for the trefoil domains in, pSP represents an unusual polypeptide fold. A striking feature of both, trefoil domains is a surface patch formed from five conserved residues, that have no obvious structural role. The two patches are located at the, far ends of the protein molecule, and we propose that these residues form, at least part of the receptor binding site, or sites, on pSP.
About this Structure
1PCP is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Solution structure of a trefoil-motif-containing cell growth factor, porcine spasmolytic protein., Carr MD, Bauer CJ, Gradwell MJ, Feeney J, Proc Natl Acad Sci U S A. 1994 Mar 15;91(6):2206-10. PMID:8134374
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