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.

1lgq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="1lgq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lgq, resolution 2.10&Aring;" /> '''Crystal structure o...)
Line 1: Line 1:
-
[[Image:1lgq.gif|left|200px]]<br />
+
[[Image:1lgq.gif|left|200px]]<br /><applet load="1lgq" size="350" color="white" frame="true" align="right" spinBox="true"
-
<applet load="1lgq" size="450" color="white" frame="true" align="right" spinBox="true"
+
caption="1lgq, resolution 2.10&Aring;" />
caption="1lgq, resolution 2.10&Aring;" />
'''Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein'''<br />
'''Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein'''<br />
==Overview==
==Overview==
-
The Chfr mitotic checkpoint protein is frequently inactivated in human, cancer. We determined the three-dimensional structure of its FHA domain in, its native form and in complex with tungstate, an analog of phosphate. The, structures revealed a beta sandwich fold similar to the previously, determined folds of the Rad53 N- and C-terminal FHA domains, except that, the Rad53 domains were monomeric, whereas the Chfr FHA domain crystallized, as a segment-swapped dimer. The ability of the Chfr FHA domain to, recognize tungstate suggests that it shares the ability with other FHA, domains to bind phosphoproteins. Nevertheless, differences in the sequence, and structure of the Chfr and Rad53 FHA domains suggest that FHA domains, can be divided into families with distinct binding properties.
+
The Chfr mitotic checkpoint protein is frequently inactivated in human cancer. We determined the three-dimensional structure of its FHA domain in its native form and in complex with tungstate, an analog of phosphate. The structures revealed a beta sandwich fold similar to the previously determined folds of the Rad53 N- and C-terminal FHA domains, except that the Rad53 domains were monomeric, whereas the Chfr FHA domain crystallized as a segment-swapped dimer. The ability of the Chfr FHA domain to recognize tungstate suggests that it shares the ability with other FHA domains to bind phosphoproteins. Nevertheless, differences in the sequence and structure of the Chfr and Rad53 FHA domains suggest that FHA domains can be divided into families with distinct binding properties.
==About this Structure==
==About this Structure==
-
1LGQ 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=1LGQ OCA].
+
1LGQ 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=1LGQ OCA].
==Reference==
==Reference==
Line 14: Line 13:
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
-
[[Category: Halazonetis, T.D.]]
+
[[Category: Halazonetis, T D.]]
[[Category: Huyen, Y.]]
[[Category: Huyen, Y.]]
-
[[Category: Jeffrey, P.D.]]
+
[[Category: Jeffrey, P D.]]
-
[[Category: Loreto, I.R.]]
+
[[Category: Loreto, I R.]]
-
[[Category: Pavletich, N.P.]]
+
[[Category: Pavletich, N P.]]
-
[[Category: Scolnick, D.M.]]
+
[[Category: Scolnick, D M.]]
-
[[Category: Stavridi, E.S.]]
+
[[Category: Stavridi, E S.]]
[[Category: checkpoint]]
[[Category: checkpoint]]
[[Category: chfr]]
[[Category: chfr]]
Line 26: Line 25:
[[Category: fha]]
[[Category: fha]]
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:00:32 2007''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:44:47 2008''

Revision as of 11:44, 21 February 2008

Image:1lgq.gif

1lgq, resolution 2.10Å

Drag the structure with the mouse to rotate

Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein

Overview

The Chfr mitotic checkpoint protein is frequently inactivated in human cancer. We determined the three-dimensional structure of its FHA domain in its native form and in complex with tungstate, an analog of phosphate. The structures revealed a beta sandwich fold similar to the previously determined folds of the Rad53 N- and C-terminal FHA domains, except that the Rad53 domains were monomeric, whereas the Chfr FHA domain crystallized as a segment-swapped dimer. The ability of the Chfr FHA domain to recognize tungstate suggests that it shares the ability with other FHA domains to bind phosphoproteins. Nevertheless, differences in the sequence and structure of the Chfr and Rad53 FHA domains suggest that FHA domains can be divided into families with distinct binding properties.

About this Structure

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

Reference

Crystal structure of the FHA domain of the Chfr mitotic checkpoint protein and its complex with tungstate., Stavridi ES, Huyen Y, Loreto IR, Scolnick DM, Halazonetis TD, Pavletich NP, Jeffrey PD, Structure. 2002 Jul;10(7):891-9. PMID:12121644

Page seeded by OCA on Thu Feb 21 13:44:47 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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