This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2iui

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="2iui" size="450" color="white" frame="true" align="right" spinBox="true" caption="2iui, resolution 2.40&Aring;" /> '''CRYSTAL STRUCTURE O...)
Line 1: Line 1:
-
[[Image:2iui.gif|left|200px]]<br />
+
[[Image:2iui.gif|left|200px]]<br /><applet load="2iui" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="2iui" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="2iui, resolution 2.40&Aring;" />
caption="2iui, resolution 2.40&Aring;" />
'''CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH PDGFR PHOSPHOTYROSYL PEPTIDE'''<br />
'''CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH PDGFR PHOSPHOTYROSYL PEPTIDE'''<br />
==Overview==
==Overview==
-
Crystal structures of the amino-terminal SH2 domain of the p85alpha, subunit of phosphatidylinositol (PI) 3-kinase, alone and in complex with, phosphopeptides bearing pTyr-Met/Val-Xaa-Met motifs, show that, phosphopeptides bind in the two-pronged manner seen in high-affinity Lck, and Src SH2 complexes, with conserved interactions between the domain and, the peptide segment from phosphotyrosine to Met+3. Peptide binding, requires the rearrangement of a tyrosyl side chain in the BG loop to, create the hydrophobic Met+3 binding pocket. The structures suggest a, mechanism for the biological specificity exhibited by PI 3-kinase in its, interactions with phosphoprotein partners.
+
Crystal structures of the amino-terminal SH2 domain of the p85alpha subunit of phosphatidylinositol (PI) 3-kinase, alone and in complex with phosphopeptides bearing pTyr-Met/Val-Xaa-Met motifs, show that phosphopeptides bind in the two-pronged manner seen in high-affinity Lck and Src SH2 complexes, with conserved interactions between the domain and the peptide segment from phosphotyrosine to Met+3. Peptide binding requires the rearrangement of a tyrosyl side chain in the BG loop to create the hydrophobic Met+3 binding pocket. The structures suggest a mechanism for the biological specificity exhibited by PI 3-kinase in its interactions with phosphoprotein partners.
==About this Structure==
==About this Structure==
-
2IUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2IUI OCA].
+
2IUI is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUI OCA].
==Reference==
==Reference==
Line 14: Line 13:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Eck, M.J.]]
+
[[Category: Eck, M J.]]
-
[[Category: Harrison, S.C.]]
+
[[Category: Harrison, S C.]]
-
[[Category: Nolte, R.T.]]
+
[[Category: Nolte, R T.]]
[[Category: Schlessinger, J.]]
[[Category: Schlessinger, J.]]
-
[[Category: Shoelson, S.E.]]
+
[[Category: Shoelson, S E.]]
[[Category: disease mutation]]
[[Category: disease mutation]]
[[Category: p85]]
[[Category: p85]]
Line 31: Line 30:
[[Category: ubl conjugation]]
[[Category: ubl conjugation]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 22:48:18 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:06 2008''

Revision as of 15:56, 21 February 2008

Image:2iui.gif

2iui, resolution 2.40Å

Drag the structure with the mouse to rotate

CRYSTAL STRUCTURE OF THE PI3-KINASE P85 N-TERMINAL SH2 DOMAIN IN COMPLEX WITH PDGFR PHOSPHOTYROSYL PEPTIDE

Overview

Crystal structures of the amino-terminal SH2 domain of the p85alpha subunit of phosphatidylinositol (PI) 3-kinase, alone and in complex with phosphopeptides bearing pTyr-Met/Val-Xaa-Met motifs, show that phosphopeptides bind in the two-pronged manner seen in high-affinity Lck and Src SH2 complexes, with conserved interactions between the domain and the peptide segment from phosphotyrosine to Met+3. Peptide binding requires the rearrangement of a tyrosyl side chain in the BG loop to create the hydrophobic Met+3 binding pocket. The structures suggest a mechanism for the biological specificity exhibited by PI 3-kinase in its interactions with phosphoprotein partners.

About this Structure

2IUI is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the PI 3-kinase p85 amino-terminal SH2 domain and its phosphopeptide complexes., Nolte RT, Eck MJ, Schlessinger J, Shoelson SE, Harrison SC, Nat Struct Biol. 1996 Apr;3(4):364-74. PMID:8599763

Page seeded by OCA on Thu Feb 21 17:56:06 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2iui"
Personal tools