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| Reference: |
Yuvaniyama J, Denu JM, Dixon JE, Saper MACrystal structure of the dual specificity protein phosphatase VHRScience v272, p.1328-1331Dual 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....
All References |
| Description: |
Human Vh1-Related Dual-Specificity Phosphatase. |
| Deposition: |
1996/2/20   |
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| Author: |
Yuvaniyama J, Denu JM, Dixon JE, Saper MA |
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| Taxonomy: |
Homo sapiens |
| Related Structure: |
VAST |
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Molecular components in the MMDB structure are listed below and may include macromolecular chains, 3D domains, protein classifications (domain families), and ligands, as available. Mouse over each icon for more information on the component.  | Ligand |
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sulfuric acid |
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1 occurrence |
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HEPES |
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1 occurrence |
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Citing MMDB:
Wang Y, Addess KJ, Chen J, Geer LY, He J, He S, Lu S, Madej T, Marchler-Bauer A, Thiessen PA, Zhang N, Bryant SH.
"MMDB: annotating protein sequences with Entrez's 3D-structure database.",
Nucleic Acids Res. 2007 Jan; 35(Database issue): D298-300.
Chen J, Anderson JB, DeWeese-Scott C, Fedorova ND, Geer LY, He S, Hurwitz DI, Jackson JD, Jacobs AR, Lanczycki CJ, Liebert CA, Liu C, Madej T, Marchler-Bauer A, Marchler GH, Mazumder R, Nikolskaya AN, Rao BS, Panchenko AR, Shoemaker BA, Simonyan V, Song JS, Thiessen PA, Vasudevan S, Wang Y, Yamashita RA, Yin JJ, Bryant SH.
"MMDB: Entrez's 3D-structure database", Nucleic Acids Res. 2003 Jan; 31(1): 474-7.
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