1d5r

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spinqualitylabelsall models PDB ID 1d5r Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image
, resolution 2.1Å
Ligands:
Activity:	Protein-tyrosine-phosphatase, with EC number 3.1.3.48
Coordinates:	save as pdb, mmCIF, xml

CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

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.

Disease

Known diseases associated with this structure: Bannayan-Riley-Ruvalcaba syndrome OMIM:[601728], Cowden disease OMIM:[601728], Endometrial carcinoma OMIM:[601728], Lhermitte-Duclos syndrome OMIM:[601728], Macrocephaly/autism s OMIM:[601728], Meningioma OMIM:[601728], Oligodendroglioma OMIM:[601728], Prostate cancer OMIM:[601728], Proteus syndrome OMIM:[601728], Thyroid carcinoma, follicular OMIM:[601728], VATER association with hydrocephalus OMIM:[601728]

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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