1oo3: Difference between revisions

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[[Image:1oo3.gif|left|200px]]<br /><applet load="1oo3" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1oo3.gif|left|200px]]<br /><applet load="1oo3" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1oo3" />

'''P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase'''<br />

==Overview==

Understanding the specificity of Src homology 2 (SH2) domains is important, because of their critical role in cell signaling. Previous genetic, analysis has characterized mutants of the N-terminal src homology 2 (SH2), domain of the p85 subunit of phosphoinositide 3-kinase (PI3K). The P395S, mutant exhibits a specificity for phosphopeptide binding different from, that of the wild-type SH2. The P395S mutant has an increased affinity for, the platelet-derived growth factor receptor (PDGFr) compared to, polyomavirus middle T antigen (MT). Solution structures of the P395S, mutant of the p85 N-SH2 alone and complexed to a PDGFr phosphopeptide were, determined to explain the change in specificity. Chemical shift, perturbations caused by different peptides were compared for mutant and, wild-type structures. The results show that the single P395S mutation has, broad effects on the structure. Furthermore, they provide a rationale for, the observed changes in binding preference.

Understanding the specificity of Src homology 2 (SH2) domains is important because of their critical role in cell signaling. Previous genetic analysis has characterized mutants of the N-terminal src homology 2 (SH2) domain of the p85 subunit of phosphoinositide 3-kinase (PI3K). The P395S mutant exhibits a specificity for phosphopeptide binding different from that of the wild-type SH2. The P395S mutant has an increased affinity for the platelet-derived growth factor receptor (PDGFr) compared to polyomavirus middle T antigen (MT). Solution structures of the P395S mutant of the p85 N-SH2 alone and complexed to a PDGFr phosphopeptide were determined to explain the change in specificity. Chemical shift perturbations caused by different peptides were compared for mutant and wild-type structures. The results show that the single P395S mutation has broad effects on the structure. Furthermore, they provide a rationale for the observed changes in binding preference.

==About this Structure==

1OO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1OO3 OCA].

1OO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OO3 OCA].

==Reference==

Line 13:

[[Category: Bos taurus]]

[[Category: Single protein]]

[[Category: Guenther, U.L.]]

[[Category: Guenther, U L.]]

[[Category: Schaffhausen, B.]]

[[Category: Weyrauch, B.]]

[[Category: src homology 2 domain p85 regulatory subunit mutant]]

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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:49 2008''

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@@ Line 1: / Line 1: @@
-[[Image:1oo3.gif|left|200px]]<br /><applet load="1oo3" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1oo3.gif|left|200px]]<br /><applet load="1oo3" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1oo3" />
 '''P395S mutant of the p85 regulatory subunit of the N-terminal src homology 2 domain of PI3-Kinase'''<br />
 ==Overview==
-Understanding the specificity of Src homology 2 (SH2) domains is important, because of their critical role in cell signaling. Previous genetic, analysis has characterized mutants of the N-terminal src homology 2 (SH2), domain of the p85 subunit of phosphoinositide 3-kinase (PI3K). The P395S, mutant exhibits a specificity for phosphopeptide binding different from, that of the wild-type SH2. The P395S mutant has an increased affinity for, the platelet-derived growth factor receptor (PDGFr) compared to, polyomavirus middle T antigen (MT). Solution structures of the P395S, mutant of the p85 N-SH2 alone and complexed to a PDGFr phosphopeptide were, determined to explain the change in specificity. Chemical shift, perturbations caused by different peptides were compared for mutant and, wild-type structures. The results show that the single P395S mutation has, broad effects on the structure. Furthermore, they provide a rationale for, the observed changes in binding preference.
+Understanding the specificity of Src homology 2 (SH2) domains is important because of their critical role in cell signaling. Previous genetic analysis has characterized mutants of the N-terminal src homology 2 (SH2) domain of the p85 subunit of phosphoinositide 3-kinase (PI3K). The P395S mutant exhibits a specificity for phosphopeptide binding different from that of the wild-type SH2. The P395S mutant has an increased affinity for the platelet-derived growth factor receptor (PDGFr) compared to polyomavirus middle T antigen (MT). Solution structures of the P395S mutant of the p85 N-SH2 alone and complexed to a PDGFr phosphopeptide were determined to explain the change in specificity. Chemical shift perturbations caused by different peptides were compared for mutant and wild-type structures. The results show that the single P395S mutation has broad effects on the structure. Furthermore, they provide a rationale for the observed changes in binding preference.
 ==About this Structure==
-OO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1OO3 OCA].
+OO3 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1OO3 OCA].
 ==Reference==
@@ Line 13: / Line 13: @@
 [[Category: Bos taurus]]
 [[Category: Single protein]]
-[[Category: Guenther, U.L.]]
+[[Category: Guenther, U L.]]
 [[Category: Schaffhausen, B.]]
 [[Category: Weyrauch, B.]]
 [[Category: src homology 2 domain p85 regulatory subunit mutant]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 23:03:22 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:19:49 2008''