1d5r
From Proteopedia
(New page: 200px<br /> <applet load="1d5r" size="450" color="white" frame="true" align="right" spinBox="true" caption="1d5r, resolution 2.1Å" /> '''CRYSTAL STRUCTURE OF...) |
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| - | [[Image:1d5r.gif|left|200px]]<br /> | + | [[Image:1d5r.gif|left|200px]]<br /><applet load="1d5r" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1d5r" size=" | + | |
caption="1d5r, resolution 2.1Å" /> | caption="1d5r, resolution 2.1Å" /> | ||
'''CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR'''<br /> | '''CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR'''<br /> | ||
==Overview== | ==Overview== | ||
| - | The PTEN tumor suppressor is mutated in diverse human cancers and in | + | 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== | ==Disease== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1D5R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with TLA as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http:// | + | 1D5R is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=TLA:'>TLA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Active as [http://en.wikipedia.org/wiki/Protein-tyrosine-phosphatase Protein-tyrosine-phosphatase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.1.3.48 3.1.3.48] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1D5R OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Cristofano, A | + | [[Category: Cristofano, A Di.]] |
| - | [[Category: Georgescu, M | + | [[Category: Georgescu, M M.]] |
| - | [[Category: Lee, J | + | [[Category: Lee, J O.]] |
| - | [[Category: Pavletich, N | + | [[Category: Pavletich, N P.]] |
[[Category: Yang, H.]] | [[Category: Yang, H.]] | ||
[[Category: TLA]] | [[Category: TLA]] | ||
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[[Category: phosphotidylinositol]] | [[Category: phosphotidylinositol]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:13:13 2008'' |
Revision as of 10:13, 21 February 2008
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CRYSTAL STRUCTURE OF THE PTEN TUMOR SUPPRESSOR
Contents |
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 with as ligand. Active as Protein-tyrosine-phosphatase, with EC number 3.1.3.48 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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