We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

1bzc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1bzc.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:1bzc.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1bzc| PDB=1bzc | SCENE= }}
{{STRUCTURE_1bzc| PDB=1bzc | SCENE= }}
-
'''HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH TPI'''
+
===HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH TPI===
-
==Overview==
+
<!--
-
Protein tyrosine phosphatases regulate diverse cellular processes and represent important targets for therapeutic intervention in a number of diseases. The crystal structures of protein tyrosine phosphatase 1B (PTP1B) in complex with small molecule inhibitors based upon two classes of phosphotyrosine mimetics, the (difluoronaphthylmethyl)phosphonic acids and the fluoromalonyl tyrosines, have been determined to resolutions greater than 2.3 A. The fluoromalonyl tyrosine residue was incorporated within a cyclic hexapeptide modeled on an autophosphorylation site of the epidermal growth factor receptor. The structure of this inhibitor bound to PTP1B represents the first crystal structure of a non-phosphonate-containing inhibitor and reveals the mechanism of phosphotyrosine mimicry by the fluoromalonyl tyrosine residue and the nature of its interactions within the catalytic site of PTP1B. In contrast to complexes of PTP1B with phosphotyrosine-containing peptides, binding of the fluoromalonyl tyrosine residue to the catalytic site of PTP1B is not accompanied by closure of the catalytic site WPD loop. Structures of PTP1B in complex with the (difluoronaphthylmethyl)phosphonic acid derivatives reveal that substitutions of the naphthalene ring modulate the mode of inhibitor binding to the catalytic site and provide the potential for enhanced inhibitor affinity and the generation of PTP-specific inhibitors. These results provide a framework for the rational design of higher affinity and more specific phosphotyrosine mimetic inhibitors of not only protein tyrosine phosphatases but also SH2 and PTB domains.
+
The line below this paragraph, {{ABSTRACT_PUBMED_9922143}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 9922143 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_9922143}}
==About this Structure==
==About this Structure==
Line 29: Line 33:
[[Category: Inhibitor complex]]
[[Category: Inhibitor complex]]
[[Category: Tyrosine phosphatase]]
[[Category: Tyrosine phosphatase]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 12:08:48 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:59:30 2008''

Revision as of 16:59, 30 June 2008

Image:1bzc.png

Template:STRUCTURE 1bzc

HUMAN PTP1B CATALYTIC DOMAIN COMPLEXED WITH TPI

Template:ABSTRACT PUBMED 9922143

About this Structure

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

Reference

Structural basis for inhibition of the protein tyrosine phosphatase 1B by phosphotyrosine peptide mimetics., Groves MR, Yao ZJ, Roller PP, Burke TR Jr, Barford D, Biochemistry. 1998 Dec 22;37(51):17773-83. PMID:9922143

Page seeded by OCA on Mon Jun 30 19:59:30 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1bzc"
Personal tools