1d5r

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{{STRUCTURE_1d5r| PDB=1d5r | SCENE= }}
{{STRUCTURE_1d5r| PDB=1d5r | SCENE= }}
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'''CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR'''
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===CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR===
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==Overview==
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The PTEN tumor suppressor is mutated in diverse human cancers and in hereditary cancer predisposition syndromes. PTEN is a phosphatase that can act on both polypeptide and phosphoinositide substrates in vitro. The PTEN structure reveals a phosphatase domain that is similar to protein phosphatases but has an enlarged active site important for the accommodation of the phosphoinositide substrate. The structure also reveals that PTEN has a C2 domain. The PTEN C2 domain binds phospholipid membranes in vitro, and mutation of basic residues that could mediate this reduces PTEN's membrane affinity and its ability to suppress the growth of glioblastoma tumor cells. The phosphatase and C2 domains associate across an extensive interface, suggesting that the C2 domain may serve to productively position the catalytic domain on the membrane.
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(as it appears on PubMed at http://www.pubmed.gov), where 10555148 is the PubMed ID number.
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{{ABSTRACT_PUBMED_10555148}}
==About this Structure==
==About this Structure==
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[[Category: Phosphotase]]
[[Category: Phosphotase]]
[[Category: Phosphotidylinositol]]
[[Category: Phosphotidylinositol]]
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Revision as of 19:29, 30 June 2008

Image:1d5r.png


PDB ID 1d5r

Drag the structure with the mouse to rotate
1d5r, resolution 2.10Å ()
Ligands:
Activity: Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Resources: FirstGlance, OCA, RCSB, PDBsum
Coordinates: save as pdb, mmCIF, xml



CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR

Template:ABSTRACT PUBMED 10555148

About this Structure

1D5R is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the PTEN tumor suppressor: implications for its phosphoinositide phosphatase activity and membrane association., Lee JO, Yang H, Georgescu MM, Di Cristofano A, Maehama T, Shi Y, Dixon JE, Pandolfi P, Pavletich NP, Cell. 1999 Oct 29;99(3):323-34. PMID:10555148

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