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.

1g6g

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /><applet load="1g6g" size="450" color="white" frame="true" align="right" spinBox="true" caption="1g6g, resolution 1.6&Aring;" /> '''X-RAY STRUCTURE OF TH...)
Line 1: Line 1:
-
[[Image:1g6g.gif|left|200px]]<br /><applet load="1g6g" size="450" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1g6g.gif|left|200px]]<br /><applet load="1g6g" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1g6g, resolution 1.6&Aring;" />
caption="1g6g, resolution 1.6&Aring;" />
'''X-RAY STRUCTURE OF THE N-TERMINAL FHA DOMAIN FROM S. CEREVISIAE RAD53P IN COMPLEX WITH A PHOSPHOTHREONINE PEPTIDE AT 1.6 A RESOLUTION'''<br />
'''X-RAY STRUCTURE OF THE N-TERMINAL FHA DOMAIN FROM S. CEREVISIAE RAD53P IN COMPLEX WITH A PHOSPHOTHREONINE PEPTIDE AT 1.6 A RESOLUTION'''<br />
==Overview==
==Overview==
-
Forkhead-associated (FHA) domains are a class of ubiquitous signaling, modules that appear to function through interactions with phosphorylated, target molecules. We have used oriented peptide library screening to, determine the optimal phosphopeptide binding motifs recognized by several, FHA domains, including those within a number of DNA damage checkpoint, kinases, and determined the X-ray structure of Rad53p-FHA1, in complex, with a phospho-threonine peptide, at 1.6 A resolution. The structure, reveals a striking similarity to the MH2 domains of Smad tumor suppressor, proteins and reveals a mode of peptide binding that differs from SH2, 14-3-3, or PTB domain complexes. These results have important implications, for DNA damage signaling and CHK2-dependent tumor suppression, and they, indicate that FHA domains play important and unsuspected roles in S/T, kinase signaling mechanisms in prokaryotes and eukaryotes.
+
Forkhead-associated (FHA) domains are a class of ubiquitous signaling modules that appear to function through interactions with phosphorylated target molecules. We have used oriented peptide library screening to determine the optimal phosphopeptide binding motifs recognized by several FHA domains, including those within a number of DNA damage checkpoint kinases, and determined the X-ray structure of Rad53p-FHA1, in complex with a phospho-threonine peptide, at 1.6 A resolution. The structure reveals a striking similarity to the MH2 domains of Smad tumor suppressor proteins and reveals a mode of peptide binding that differs from SH2, 14-3-3, or PTB domain complexes. These results have important implications for DNA damage signaling and CHK2-dependent tumor suppression, and they indicate that FHA domains play important and unsuspected roles in S/T kinase signaling mechanisms in prokaryotes and eukaryotes.
==About this Structure==
==About this Structure==
-
1G6G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1G6G OCA].
+
1G6G is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1G6G OCA].
==Reference==
==Reference==
Line 14: Line 14:
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Durocher, D.]]
[[Category: Durocher, D.]]
-
[[Category: Taylor, I.A.]]
+
[[Category: Taylor, I A.]]
[[Category: beta-sandwich]]
[[Category: beta-sandwich]]
[[Category: phosphopeptide complex]]
[[Category: phosphopeptide complex]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 15:45:11 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:46:40 2008''

Revision as of 10:46, 21 February 2008

Image:1g6g.gif

1g6g, resolution 1.6Å

Drag the structure with the mouse to rotate

X-RAY STRUCTURE OF THE N-TERMINAL FHA DOMAIN FROM S. CEREVISIAE RAD53P IN COMPLEX WITH A PHOSPHOTHREONINE PEPTIDE AT 1.6 A RESOLUTION

Overview

Forkhead-associated (FHA) domains are a class of ubiquitous signaling modules that appear to function through interactions with phosphorylated target molecules. We have used oriented peptide library screening to determine the optimal phosphopeptide binding motifs recognized by several FHA domains, including those within a number of DNA damage checkpoint kinases, and determined the X-ray structure of Rad53p-FHA1, in complex with a phospho-threonine peptide, at 1.6 A resolution. The structure reveals a striking similarity to the MH2 domains of Smad tumor suppressor proteins and reveals a mode of peptide binding that differs from SH2, 14-3-3, or PTB domain complexes. These results have important implications for DNA damage signaling and CHK2-dependent tumor suppression, and they indicate that FHA domains play important and unsuspected roles in S/T kinase signaling mechanisms in prokaryotes and eukaryotes.

About this Structure

1G6G is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

The molecular basis of FHA domain:phosphopeptide binding specificity and implications for phospho-dependent signaling mechanisms., Durocher D, Taylor IA, Sarbassova D, Haire LF, Westcott SL, Jackson SP, Smerdon SJ, Yaffe MB, Mol Cell. 2000 Nov;6(5):1169-82. PMID:11106755

Page seeded by OCA on Thu Feb 21 12:46:40 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1g6g"
Personal tools