1klq

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==Overview==
==Overview==
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Mad2 participates in spindle checkpoint inhibition of APC(Cdc20). We show, that RNAi-mediated suppression of Mad1 function in mammalian cells causes, loss of Mad2 kinetochore localization and impairment of the spindle, checkpoint. Mad1 and Cdc20 contain Mad2 binding motifs that share a common, consensus. We have identified a class of Mad2 binding peptides with a, similar consensus. Binding of one of these ligands, MBP1, triggers an, extensive rearrangement of the tertiary structure of Mad2. Mad2 also, undergoes a similar striking structural change upon binding to a Mad1 or, Cdc20 binding motif peptide. Our data suggest that, upon checkpoint, activation, Mad1 recruits Mad2 to unattached kinetochores and may promote, binding of Mad2 to Cdc20.
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Mad2 participates in spindle checkpoint inhibition of APC(Cdc20). We show that RNAi-mediated suppression of Mad1 function in mammalian cells causes loss of Mad2 kinetochore localization and impairment of the spindle checkpoint. Mad1 and Cdc20 contain Mad2 binding motifs that share a common consensus. We have identified a class of Mad2 binding peptides with a similar consensus. Binding of one of these ligands, MBP1, triggers an extensive rearrangement of the tertiary structure of Mad2. Mad2 also undergoes a similar striking structural change upon binding to a Mad1 or Cdc20 binding motif peptide. Our data suggest that, upon checkpoint activation, Mad1 recruits Mad2 to unattached kinetochores and may promote binding of Mad2 to Cdc20.
==About this Structure==
==About this Structure==
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[[Category: protein-peptide complex]]
[[Category: protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:14:34 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:35:30 2008''

Revision as of 11:35, 21 February 2008


1klq

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The Mad2 Spindle Checkpoint Protein Undergoes Similar Major Conformational Changes upon Binding to Either Mad1 or Cdc20

Overview

Mad2 participates in spindle checkpoint inhibition of APC(Cdc20). We show that RNAi-mediated suppression of Mad1 function in mammalian cells causes loss of Mad2 kinetochore localization and impairment of the spindle checkpoint. Mad1 and Cdc20 contain Mad2 binding motifs that share a common consensus. We have identified a class of Mad2 binding peptides with a similar consensus. Binding of one of these ligands, MBP1, triggers an extensive rearrangement of the tertiary structure of Mad2. Mad2 also undergoes a similar striking structural change upon binding to a Mad1 or Cdc20 binding motif peptide. Our data suggest that, upon checkpoint activation, Mad1 recruits Mad2 to unattached kinetochores and may promote binding of Mad2 to Cdc20.

About this Structure

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

Reference

The Mad2 spindle checkpoint protein undergoes similar major conformational changes upon binding to either Mad1 or Cdc20., Luo X, Tang Z, Rizo J, Yu H, Mol Cell. 2002 Jan;9(1):59-71. PMID:11804586

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