1pcp
From Proteopedia
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| - | [[Image:1pcp.gif|left|200px]] | + | [[Image:1pcp.gif|left|200px]] |
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| - | '''SOLUTION STRUCTURE OF A TREFOIL-MOTIF-CONTAINING CELL GROWTH FACTOR, PORCINE SPASMOLYTIC PROTEIN''' | + | {{Structure |
| + | |PDB= 1pcp |SIZE=350|CAPTION= <scene name='initialview01'>1pcp</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
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| + | '''SOLUTION STRUCTURE OF A TREFOIL-MOTIF-CONTAINING CELL GROWTH FACTOR, PORCINE SPASMOLYTIC PROTEIN''' | ||
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==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1PCP is a [ | + | 1PCP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1PCP OCA]. |
==Reference== | ==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:[http:// | + | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8134374 8134374] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: growth factor]] | [[Category: growth factor]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:22:45 2008'' |
Revision as of 11:22, 20 March 2008
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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
Page seeded by OCA on Thu Mar 20 13:22:45 2008
