1x24: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1x24.gif|left|200px]] | [[Image:1x24.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1x24", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
or leave the SCENE parameter empty for the default display. | |||
| | --> | ||
| | {{STRUCTURE_1x24| PDB=1x24 | SCENE= }} | ||
}} | |||
'''Prl-1 (ptp4a)''' | '''Prl-1 (ptp4a)''' | ||
| Line 31: | Line 28: | ||
[[Category: Yang, H.]] | [[Category: Yang, H.]] | ||
[[Category: Zhang, Z Y.]] | [[Category: Zhang, Z Y.]] | ||
[[Category: | [[Category: Dual specific phosphatase]] | ||
[[Category: | [[Category: Prl-1]] | ||
[[Category: | [[Category: Tyrosine phosphatase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 14:25:53 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 14:25, 3 May 2008
Prl-1 (ptp4a)
OverviewOverview
The PRL (phosphatase of regenerating liver) phosphatases constitute a novel class of small, prenylated phosphatases that are implicated in promoting cell growth, differentiation, and tumor invasion, and represent attractive targets for anticancer therapy. Here we describe the crystal structures of native PRL-1 as well as the catalytically inactive mutant PRL-1/C104S in complex with sulfate. PRL-1 exists as a trimer in the crystalline state, burying 1140 A2 of accessible surface area at each dimer interface. Trimerization creates a large, bipartite membrane-binding surface in which the exposed C-terminal basic residues could cooperate with the adjacent prenylation group to anchor PRL-1 on the acidic inner membrane. Structural and kinetic analyses place PRL-1 in the family of dual specificity phopsphatases with closest structural similarity to the Cdc14 phosphatase and provide a molecular basis for catalytic activation of the PRL phosphatases. Finally, native PRL-1 is crystallized in an oxidized form in which a disulfide is formed between the active site Cys104 and a neighboring residue Cys49, which blocks both substrate binding and catalysis. Biochemical studies in solution and in the cell support a potential regulatory role of this intramolecular disulfide bond formation in response to reactive oxygen species such as H2O2.
About this StructureAbout this Structure
1X24 is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
ReferenceReference
Structure and biochemical properties of PRL-1, a phosphatase implicated in cell growth, differentiation, and tumor invasion., Sun JP, Wang WQ, Yang H, Liu S, Liang F, Fedorov AA, Almo SC, Zhang ZY, Biochemistry. 2005 Sep 13;44(36):12009-21. PMID:16142898 Page seeded by OCA on Sat May 3 14:25:53 2008