1bvh: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1bvh.gif|left|200px]] | [[Image:1bvh.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1bvh", 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_1bvh| PDB=1bvh | SCENE= }} | ||
}} | |||
'''SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE''' | '''SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE''' | ||
| Line 32: | Line 29: | ||
[[Category: Nettesheim, D G.]] | [[Category: Nettesheim, D G.]] | ||
[[Category: Zhou, M M.]] | [[Category: Zhou, M M.]] | ||
[[Category: | [[Category: Hydrolase]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:00:04 2008'' | |||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 12:00, 2 May 2008
SOLUTION STRUCTURE OF A LOW MOLECULAR WEIGHT PROTEIN TYROSINE PHOSPHATASE
OverviewOverview
Protein tyrosine phosphatases (PTPs) are important enzymes involved in signal transduction, cell cycle regulation, and the control of differentiation. Despite the importance of this class of enzymes in the control of critical cell processes, very little structural information is available for this family of proteins. In this paper, we present the first solution structure of a protein tyrosine phosphatase. This protein is a low molecular weight cytosolic PTP that was initially isolated from bovine heart. The structure that was determined from 1747 NMR-derived restraints consists of a central four-stranded parallel beta-sheet surrounded by four alpha-helices and a short 3(10) helix. The phosphate binding site, identified by chemical shift changes upon the addition of the competitive inhibitors phosphate and vanadate, is in a loop region connecting the C-terminal end of the first beta-strand with the first alpha-helix. Residues in the second, fourth, and fifth alpha-helices and in some of the loop regions connecting the elements of regular secondary structure also contribute to the binding site. The structure determined here is consistent with previous mutagenesis and chemical modification studies conducted on this protein.
About this StructureAbout this Structure
1BVH is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of a low molecular weight protein tyrosine phosphatase., Logan TM, Zhou MM, Nettesheim DG, Meadows RP, Van Etten RL, Fesik SW, Biochemistry. 1994 Sep 20;33(37):11087-96. PMID:7727361 Page seeded by OCA on Fri May 2 12:00:04 2008