1pcp

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[[Image:1pcp.gif|left|200px]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1pcp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1pcp OCA], [http://www.ebi.ac.uk/pdbsum/1pcp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1pcp RCSB]</span>
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'''SOLUTION STRUCTURE OF A TREFOIL-MOTIF-CONTAINING CELL GROWTH FACTOR, PORCINE SPASMOLYTIC PROTEIN'''
'''SOLUTION STRUCTURE OF A TREFOIL-MOTIF-CONTAINING CELL GROWTH FACTOR, PORCINE SPASMOLYTIC PROTEIN'''
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[[Category: Feeney, J.]]
[[Category: Feeney, J.]]
[[Category: Gradwell, M J.]]
[[Category: Gradwell, M J.]]
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[[Category: growth factor]]
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[[Category: Growth factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 04:56:35 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:57:54 2008''
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Revision as of 01:56, 3 May 2008

Template:STRUCTURE 1pcp

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 Page seeded by OCA on Sat May 3 04:56:35 2008

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