1vhr
From Proteopedia
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- | [[Image:1vhr.gif|left|200px]] | + | [[Image:1vhr.gif|left|200px]] |
- | + | ||
- | '''HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE''' | + | {{Structure |
+ | |PDB= 1vhr |SIZE=350|CAPTION= <scene name='initialview01'>1vhr</scene>, resolution 2.1Å | ||
+ | |SITE= <scene name='pdbsite=GAA:The+Loop+Containing+The+Putative+General+Acid+ASP+92'>GAA</scene>, <scene name='pdbsite=GAB:The+Loop+Containing+The+Putative+General+Acid+ASP+92'>GAB</scene>, <scene name='pdbsite=PLA:Phosphate+Binding+Loop+Including+Catalytic+Nucleophile+C+...'>PLA</scene>, <scene name='pdbsite=PLB:Phosphate+Binding+Loop+Including+Catalytic+Nucleophile+C+...'>PLB</scene>, <scene name='pdbsite=RCA:Designated+Recognition+Region+In+Primary+Reference.+Prop+...'>RCA</scene>, <scene name='pdbsite=RCB:Designated+Recognition+Region+In+Primary+Reference.+Prop+...'>RCB</scene>, <scene name='pdbsite=VRA:The+Region+Containing+High+Variation+Among+The+Dual-Spec+...'>VRA</scene> and <scene name='pdbsite=VRB:The+Region+Containing+High+Variation+Among+The+Dual-Spec+...'>VRB</scene> | ||
+ | |LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=EPE:4-(2-HYDROXYETHYL)-1-PIPERAZINE ETHANESULFONIC ACID'>EPE</scene> | ||
+ | |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= | ||
+ | }} | ||
+ | |||
+ | '''HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE''' | ||
+ | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
- | 1VHR is a [ | + | 1VHR 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=1VHR OCA]. |
==Reference== | ==Reference== | ||
- | Crystal structure of the dual specificity protein phosphatase VHR., Yuvaniyama J, Denu JM, Dixon JE, Saper MA, Science. 1996 May 31;272(5266):1328-31. PMID:[http:// | + | Crystal structure of the dual specificity protein phosphatase VHR., Yuvaniyama J, Denu JM, Dixon JE, Saper MA, Science. 1996 May 31;272(5266):1328-31. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8650541 8650541] |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein-tyrosine-phosphatase]] | [[Category: Protein-tyrosine-phosphatase]] | ||
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[[Category: protein dual-specificity phosphatase]] | [[Category: protein dual-specificity phosphatase]] | ||
- | ''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 14:45:47 2008'' |
Revision as of 12:45, 20 March 2008
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, resolution 2.1Å | |||||||
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Sites: | , , , , , , and | ||||||
Ligands: | and | ||||||
Activity: | Protein-tyrosine-phosphatase, with EC number 3.1.3.48 | ||||||
Coordinates: | save as pdb, mmCIF, xml |
HUMAN VH1-RELATED DUAL-SPECIFICITY PHOSPHATASE
Overview
Dual specificity protein phosphatases (DSPs) regulate mitogenic signal transduction and control the cell cycle. Here, the crystal structure of a human DSP, vaccinia H1-related phosphatase (or VHR), was determined at 2.1 angstrom resolution. A shallow active site pocket in VHR allows for the hydrolysis of phosphorylated serine, threonine, or tyrosine protein residues, whereas the deeper active site of protein tyrosine phosphatases (PTPs) restricts substrate specificity to only phosphotyrosine. Positively charged crevices near the active site may explain the enzyme's preference for substrates with two phosphorylated residues. The VHR structure defines a conserved structural scaffold for both DSPs and PTPs. A "recognition region," connecting helix alpha1 to strand beta1, may determine differences in substrate specificity between VHR, the PTPs, and other DSPs.
About this Structure
1VHR is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Crystal structure of the dual specificity protein phosphatase VHR., Yuvaniyama J, Denu JM, Dixon JE, Saper MA, Science. 1996 May 31;272(5266):1328-31. PMID:8650541
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