1gfy

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1gfy.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1gfy.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1gfy| PDB=1gfy | SCENE= }}
{{STRUCTURE_1gfy| PDB=1gfy | SCENE= }}
-
'''RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITY OF PROTEIN-TYROSINE PHOSPHATASE 1B AND ALPHA'''
+
===RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITY OF PROTEIN-TYROSINE PHOSPHATASE 1B AND ALPHA===
-
==Overview==
+
<!--
-
The aim of this study was to define the structural elements that determine the differences in substrate recognition capacity of two protein-tyrosine phosphatases (PTPs), PTP1B and PTPalpha, both suggested to be negative regulators of insulin signaling. Since the Ac-DADE(pY)L-NH(2) peptide is well recognized by PTP1B, but less efficiently by PTPalpha, it was chosen as a tool for these analyses. Calpha regiovariation analyses and primary sequence alignments indicate that residues 47, 48, 258, and 259 (PTP1B numbering) define a selectivity-determining region. By analyzing a set of DADE(pY)L analogs with a series of PTP mutants in which these four residues were exchanged between PTP1B and PTPalpha, either in combination or alone, we here demonstrate that the key selectivity-determining residue is 259. In PTPalpha, this residue is a glutamine causing steric hindrance and in PTP1B a glycine allowing broad substrate recognition. Significantly, replacing Gln(259) with a glycine almost turns PTPalpha into a PTP1B-like enzyme. By using a novel set of PTP inhibitors and x-ray crystallography, we further provide evidence that Gln(259) in PTPalpha plays a dual role leading to restricted substrate recognition (directly via steric hindrance) and reduced catalytic activity (indirectly via Gln(262)). Both effects may indicate that PTPalpha regulates highly selective signal transduction processes.
+
The line below this paragraph, {{ABSTRACT_PUBMED_10748206}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 10748206 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_10748206}}
==About this Structure==
==About this Structure==
Line 25: Line 29:
[[Category: Iversen, L F.]]
[[Category: Iversen, L F.]]
[[Category: Hydrolase]]
[[Category: Hydrolase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 17:30:55 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 05:13:22 2008''

Revision as of 02:13, 1 July 2008

Template:STRUCTURE 1gfy

RESIDUE 259 IS A KEY DETERMINANT OF SUBSTRATE SPECIFICITY OF PROTEIN-TYROSINE PHOSPHATASE 1B AND ALPHA

Template:ABSTRACT PUBMED 10748206

About this Structure

1GFY is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Residue 259 is a key determinant of substrate specificity of protein-tyrosine phosphatases 1B and alpha., Peters GH, Iversen LF, Branner S, Andersen HS, Mortensen SB, Olsen OH, Moller KB, Moller NP, J Biol Chem. 2000 Jun 16;275(24):18201-9. PMID:10748206

Page seeded by OCA on Tue Jul 1 05:13:22 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools