1g1f: Difference between revisions

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[[Image:1g1f.~~gif~~|left|200px]]

[[Image:1g1f.png|left|200px]]

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~~'''~~CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A TRI-PHOSPHORYLATED PEPTIDE (RDI(PTR)ETD(PTR)(PTR)RK) FROM THE INSULIN RECEPTOR KINASE~~'''~~

===CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A TRI-PHOSPHORYLATED PEPTIDE (RDI(PTR)ETD(PTR)(PTR)RK) FROM THE INSULIN RECEPTOR KINASE===

~~==Overview==~~

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The ~~protein tyrosine phosphatase PTP1B is responsible for negatively regulating insulin signaling by dephosphorylating~~ the ~~phosphotyrosine residues of~~ the ~~insulin receptor kinase~~ (~~IRK~~) ~~activation segment. Here, by integrating crystallographic, kinetic~~, and PTP1B peptide binding studies, we define the molecular specificity of this reaction. Extensive interactions are formed between PTP1B and the IRK sequence encompassing the tandem pTyr residues at 1162 and 1163 such that pTyr-1162 is ~~selected at~~ the ~~catalytic site and pTyr-1163 is located within an adjacent pTyr recognition site~~. ~~This selectivity is attributed to the 70~~-~~fold greater affinity for tandem pTyr~~-containing peptides relative to mono-pTyr peptides and predicts a hierarchical dephosphorylation process. Many elements of the PTP1B-IRK interaction are unique to PTP1B, indicating that it may be feasible to generate specific, small molecule inhibitors of this interaction to treat diabetes and obesity.

The line below this paragraph, {{ABSTRACT_PUBMED_11163213}}, adds the Publication Abstract to the page

(as it appears on PubMed at http://www.pubmed.gov), where 11163213 is the PubMed ID number.

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==About this Structure==

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[[Category: Peptide complex]]

[[Category: Tyrosine phosphatase]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri May~~ ~~2 17~~:00:51 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 1 04:15:45 2008''

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-[[Image:1g1f.gif|left|200px]]
+{{Seed}}
+[[Image:1g1f.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1g1f|  PDB=1g1f  |  SCENE=  }}
-'''CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A TRI-PHOSPHORYLATED PEPTIDE (RDI(PTR)ETD(PTR)(PTR)RK) FROM THE INSULIN RECEPTOR KINASE'''
+===CRYSTAL STRUCTURE OF PROTEIN TYROSINE PHOSPHATASE 1B COMPLEXED WITH A TRI-PHOSPHORYLATED PEPTIDE (RDI(PTR)ETD(PTR)(PTR)RK) FROM THE INSULIN RECEPTOR KINASE===
-==Overview==
+<!--
-The protein tyrosine phosphatase PTP1B is responsible for negatively regulating insulin signaling by dephosphorylating the phosphotyrosine residues of the insulin receptor kinase (IRK) activation segment. Here, by integrating crystallographic, kinetic, and PTP1B peptide binding studies, we define the molecular specificity of this reaction. Extensive interactions are formed between PTP1B and the IRK sequence encompassing the tandem pTyr residues at 1162 and 1163 such that pTyr-1162 is selected at the catalytic site and pTyr-1163 is located within an adjacent pTyr recognition site. This selectivity is attributed to the 70-fold greater affinity for tandem pTyr-containing peptides relative to mono-pTyr peptides and predicts a hierarchical dephosphorylation process. Many elements of the PTP1B-IRK interaction are unique to PTP1B, indicating that it may be feasible to generate specific, small molecule inhibitors of this interaction to treat diabetes and obesity.
+The line below this paragraph, {{ABSTRACT_PUBMED_11163213}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 11163213 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_11163213}}
 ==About this Structure==
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 [[Category: Peptide complex]]
 [[Category: Tyrosine phosphatase]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 17:00:51 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul  1 04:15:45 2008''