1r6h: Difference between revisions
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'''Solution Structure of human PRL-3''' | {{Structure | ||
|PDB= 1r6h |SIZE=350|CAPTION= <scene name='initialview01'>1r6h</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= [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] | |||
|GENE= | |||
}} | |||
'''Solution Structure of human PRL-3''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1R6H is a [ | 1R6H is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R6H OCA]. | ||
==Reference== | ==Reference== | ||
Structural insights into molecular function of the metastasis-associated phosphatase PRL-3., Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I, J Biol Chem. 2004 Mar 19;279(12):11882-9. Epub 2004 Jan 1. PMID:[http:// | Structural insights into molecular function of the metastasis-associated phosphatase PRL-3., Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I, J Biol Chem. 2004 Mar 19;279(12):11882-9. Epub 2004 Jan 1. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14704153 14704153] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
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[[Category: dual specificity phosphatase fold]] | [[Category: dual specificity phosphatase fold]] | ||
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Revision as of 14:47, 20 March 2008
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| Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
Solution Structure of human PRL-3
OverviewOverview
Phosphatases and kinases are the cellular signal transduction enzymes that control protein phosphorylation. PRL phosphatases constitute a novel class of small (20 kDa), prenylated phosphatases with oncogenic activity. In particular, PRL-3 is consistently overexpressed in liver metastasis in colorectal cancer cells and represents a new therapeutic target. Here, we present the solution structure of PRL-3, the first structure of a PRL phosphatase. The structure places PRL phosphatases in the class of dual specificity phosphatases with closest structural homology to the VHR phosphatase. The structure, coupled with kinetic studies of site-directed mutants, identifies functionally important residues and reveals unique features, differentiating PRLs from other phosphatases. These differences include an unusually hydrophobic active site without the catalytically important serine/threonine found in most other phosphatases. The position of the general acid loop indicates the presence of conformational change upon catalysis. The studies also identify a potential regulatory role of Cys(49) that forms an intramolecular disulfide bond with the catalytic Cys(104) even under mildly reducing conditions. Molecular modeling of the highly homologous PRL-1 and PRL-2 phosphatases revealed unique surface elements that are potentially important for specificity.
About this StructureAbout this Structure
1R6H is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Structural insights into molecular function of the metastasis-associated phosphatase PRL-3., Kozlov G, Cheng J, Ziomek E, Banville D, Gehring K, Ekiel I, J Biol Chem. 2004 Mar 19;279(12):11882-9. Epub 2004 Jan 1. PMID:14704153
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