1psp
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(New page: 200px<br /><applet load="1psp" size="450" color="white" frame="true" align="right" spinBox="true" caption="1psp, resolution 2.5Å" /> '''PANCREATIC SPASMOLYTI...)
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Revision as of 21:58, 20 November 2007
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PANCREATIC SPASMOLYTIC POLYPEPTIDE: FIRST THREE-DIMENSIONAL STRUCTURE OF A MEMBER OF THE MAMMALIAN TREFOIL FAMILY OF PEPTIDES
Overview
BACKGROUND: The trefoil peptides are a rapidly growing family of peptides, mainly found in the gastrointestinal tract. There is circumstantial, evidence that they stabilize the mucus layer, and may affect the rate of, healing of the mucosal epithelium. RESULTS: We have determined the, structure of porcine pancreatic spasmolytic polypeptide (PSP) to 2.5 A, resolution. The polypeptide contains two trefoil domains. The domain, structure is compact, and is composed of a central short antiparallel, beta-sheet with one short helix above and one below it. This is a novel, motif. The two domains are related by two-fold symmetry, and each domain, contains a cleft. CONCLUSIONS: The cleft within each domain could, accommodate a polysaccharide chain, and may therefore be responsible for, binding mucin glycoproteins. We suggest that PSP may cross-link, glycoproteins, explaining its ability to stabilize the mucus layer.
About this Structure
1PSP is a Single protein structure of sequence from Sus scrofa. Full crystallographic information is available from OCA.
Reference
Pancreatic spasmolytic polypeptide: first three-dimensional structure of a member of the mammalian trefoil family of peptides., Gajhede M, Petersen TN, Henriksen A, Petersen JF, Dauter Z, Wilson KS, Thim L, Structure. 1993 Dec 15;1(4):253-62. PMID:8081739
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