1KLQ

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

Summary for 1KLQ

• Entry DOI: 10.2210/pdb1klq/pdb
• Related: 1DUJ
• NMR Information: BMRB: 5299
• Descriptor: MITOTIC SPINDLE ASSEMBLY CHECKPOINT PROTEIN MAD2A, Mad2-binding peptide (2 entities in total)
• Functional Keywords: protein-peptide complex, mad2 family, cell cycle
• Biological source: Homo sapiens (human); More
• Cellular location: Nucleus: Q13257
• Total number of polymer chains: 2
• Total formula weight: 24014.33

Authors

Luo, X.,Tang, Z.,Rizo, J.,Yu, H. (deposition date: 2001-12-12, release date: 2002-01-25, Last modification date: 2024-05-22)

Primary citation

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

PubMed Abstract: 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.

PubMed: 11804586
DOI: 10.1016/S1097-2765(01)00435-X

Experimental method

SOLUTION NMR