2qyf: Difference between revisions

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==Overview==

The status of spindle checkpoint signaling depends on the balance of two, opposing dynamic processes that regulate the highly unusual two-state, behavior of Mad2. In mitosis, a Mad1-Mad2 core complex recruits cytosolic, Mad2 to kinetochores through Mad2 dimerization and converts Mad2 to a, conformer amenable to Cdc20 binding, thereby facilitating checkpoint, activation. p31(comet) inactivates the checkpoint through binding to Mad1-, or Cdc20-bound Mad2, thereby preventing Mad2 activation and promoting the, dissociation of the Mad2-Cdc20 complex. Here, we report the crystal, structure of the Mad2-p31(comet) complex. The C-terminal region of Mad2, that undergoes rearrangement in different Mad2 conformers is a major, structural determinant for p31(comet) binding, explaining the specificity, of p31(comet) toward Mad1- or Cdc20-bound Mad2. p31(comet) adopts a fold, strikingly similar to that of Mad2 and binds at the dimerization interface, of Mad2. Thus, p31(comet) exploits the two-state behavior of Mad2 to block, its activation by acting as an "anti-Mad2."

The status of spindle checkpoint signaling depends on the balance of two opposing dynamic processes that regulate the highly unusual two-state behavior of Mad2. In mitosis, a Mad1-Mad2 core complex recruits cytosolic Mad2 to kinetochores through Mad2 dimerization and converts Mad2 to a conformer amenable to Cdc20 binding, thereby facilitating checkpoint activation. p31(comet) inactivates the checkpoint through binding to Mad1- or Cdc20-bound Mad2, thereby preventing Mad2 activation and promoting the dissociation of the Mad2-Cdc20 complex. Here, we report the crystal structure of the Mad2-p31(comet) complex. The C-terminal region of Mad2 that undergoes rearrangement in different Mad2 conformers is a major structural determinant for p31(comet) binding, explaining the specificity of p31(comet) toward Mad1- or Cdc20-bound Mad2. p31(comet) adopts a fold strikingly similar to that of Mad2 and binds at the dimerization interface of Mad2. Thus, p31(comet) exploits the two-state behavior of Mad2 to block its activation by acting as an "anti-Mad2."

==About this Structure==

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[[Category: Protein complex]]

[[Category: Luo, X.]]

[[Category: Tomchick, D.R.]]

[[Category: Tomchick, D R.]]

[[Category: cell cycle]]

[[Category: cell division]]

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[[Category: spindle assembly checkpoint]]

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu ~~Jan 31 10~~:59:21 2008''

''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:43:19 2008''

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@@ Line 4: / Line 4: @@
 ==Overview==
-The status of spindle checkpoint signaling depends on the balance of two, opposing dynamic processes that regulate the highly unusual two-state, behavior of Mad2. In mitosis, a Mad1-Mad2 core complex recruits cytosolic, Mad2 to kinetochores through Mad2 dimerization and converts Mad2 to a, conformer amenable to Cdc20 binding, thereby facilitating checkpoint, activation. p31(comet) inactivates the checkpoint through binding to Mad1-, or Cdc20-bound Mad2, thereby preventing Mad2 activation and promoting the, dissociation of the Mad2-Cdc20 complex. Here, we report the crystal, structure of the Mad2-p31(comet) complex. The C-terminal region of Mad2, that undergoes rearrangement in different Mad2 conformers is a major, structural determinant for p31(comet) binding, explaining the specificity, of p31(comet) toward Mad1- or Cdc20-bound Mad2. p31(comet) adopts a fold, strikingly similar to that of Mad2 and binds at the dimerization interface, of Mad2. Thus, p31(comet) exploits the two-state behavior of Mad2 to block, its activation by acting as an "anti-Mad2."
+The status of spindle checkpoint signaling depends on the balance of two opposing dynamic processes that regulate the highly unusual two-state behavior of Mad2. In mitosis, a Mad1-Mad2 core complex recruits cytosolic Mad2 to kinetochores through Mad2 dimerization and converts Mad2 to a conformer amenable to Cdc20 binding, thereby facilitating checkpoint activation. p31(comet) inactivates the checkpoint through binding to Mad1- or Cdc20-bound Mad2, thereby preventing Mad2 activation and promoting the dissociation of the Mad2-Cdc20 complex. Here, we report the crystal structure of the Mad2-p31(comet) complex. The C-terminal region of Mad2 that undergoes rearrangement in different Mad2 conformers is a major structural determinant for p31(comet) binding, explaining the specificity of p31(comet) toward Mad1- or Cdc20-bound Mad2. p31(comet) adopts a fold strikingly similar to that of Mad2 and binds at the dimerization interface of Mad2. Thus, p31(comet) exploits the two-state behavior of Mad2 to block its activation by acting as an "anti-Mad2."
 ==About this Structure==
@@ Line 14: / Line 14: @@
 [[Category: Protein complex]]
 [[Category: Luo, X.]]
-[[Category: Tomchick, D.R.]]
+[[Category: Tomchick, D R.]]
 [[Category: cell cycle]]
 [[Category: cell division]]
@@ Line 24: / Line 24: @@
 [[Category: spindle assembly checkpoint]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Jan 31 10:59:21 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 18:43:19 2008''