1duj: Difference between revisions

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==Overview==

The checkpoint protein Mad2 inhibits the activity of the anaphase, promoting complex by sequestering Cdc20 until all chromosomes are aligned, at the metaphase plate. We report the solution structure of human Mad2 and, its interaction with Cdc20. Mad2 possesses a novel three-layered, alpha/beta fold with three alpha-helices packed between two beta-sheets., Using deletion mutants we identified the minimal Mad2-binding region of, human Cdc20 as a 40-residue segment immediately N-terminal to the WD40, repeats. Mutagenesis and NMR titration experiments show that a C-terminal, flexible region of Mad2 is required for binding to Cdc20. Mad2 and Cdc20, form a tight 1:1 heterodimeric complex in which the C-terminal segment of, Mad2 becomes folded. These results provide the first structural insight, into mechanisms of the spindle assembly checkpoint.

The checkpoint protein Mad2 inhibits the activity of the anaphase promoting complex by sequestering Cdc20 until all chromosomes are aligned at the metaphase plate. We report the solution structure of human Mad2 and its interaction with Cdc20. Mad2 possesses a novel three-layered alpha/beta fold with three alpha-helices packed between two beta-sheets. Using deletion mutants we identified the minimal Mad2-binding region of human Cdc20 as a 40-residue segment immediately N-terminal to the WD40 repeats. Mutagenesis and NMR titration experiments show that a C-terminal flexible region of Mad2 is required for binding to Cdc20. Mad2 and Cdc20 form a tight 1:1 heterodimeric complex in which the C-terminal segment of Mad2 becomes folded. These results provide the first structural insight into mechanisms of the spindle assembly checkpoint.

==About this Structure==

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[[Category: spindle assembly checkpoint]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Fri~~ Feb ~~15 15~~:40:50 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:36 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The checkpoint protein Mad2 inhibits the activity of the anaphase, promoting complex by sequestering Cdc20 until all chromosomes are aligned, at the metaphase plate. We report the solution structure of human Mad2 and, its interaction with Cdc20. Mad2 possesses a novel three-layered, alpha/beta fold with three alpha-helices packed between two beta-sheets., Using deletion mutants we identified the minimal Mad2-binding region of, human Cdc20 as a 40-residue segment immediately N-terminal to the WD40, repeats. Mutagenesis and NMR titration experiments show that a C-terminal, flexible region of Mad2 is required for binding to Cdc20. Mad2 and Cdc20, form a tight 1:1 heterodimeric complex in which the C-terminal segment of, Mad2 becomes folded. These results provide the first structural insight, into mechanisms of the spindle assembly checkpoint.
+The checkpoint protein Mad2 inhibits the activity of the anaphase promoting complex by sequestering Cdc20 until all chromosomes are aligned at the metaphase plate. We report the solution structure of human Mad2 and its interaction with Cdc20. Mad2 possesses a novel three-layered alpha/beta fold with three alpha-helices packed between two beta-sheets. Using deletion mutants we identified the minimal Mad2-binding region of human Cdc20 as a 40-residue segment immediately N-terminal to the WD40 repeats. Mutagenesis and NMR titration experiments show that a C-terminal flexible region of Mad2 is required for binding to Cdc20. Mad2 and Cdc20 form a tight 1:1 heterodimeric complex in which the C-terminal segment of Mad2 becomes folded. These results provide the first structural insight into mechanisms of the spindle assembly checkpoint.
 ==About this Structure==
@@ Line 21: / Line 21: @@
 [[Category: spindle assembly checkpoint]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:40:50 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:20:36 2008''