Cat. No.

CBCRY03

Background

The crystal structure of the Mad2-p31(comet) complex is reported. 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."

Molecular description

Protein Classification

cell cycle

Structure Weight

105471.24 Da

Polymer

1

Molecule

Mitotic spindle assembly checkpoint protein MAD2A

Chain Length

210 amino acids

Polymer

2

Molecule

MAD2L1-binding protein

Chain Length

268 amino acids

Polymer

3

Molecule

peptide

Chain Length

12 amino acids

Crystal Description

PDB ID

2QYF

Source

E.coli

Method

X-Ray Diffraction

Resolution

2.30 Å

Modified residues

selenomethionine (pareint: MET)

Gene information

Gene Name

MAD2L1

Synonyms

HSMAD2; MAD2; MAD2 (mitotic arrest deficient, yeast, homolog)-like 1; MAD2-like 1; MAD2-like protein 1; mitotic arrest deficient, yeast, homolog-like 1

UniProt ID

Q13257

GeneID

4085

Chromosome  Location

4q27

Function

protein binding

Gene Name

MAD2L1BP

Synonyms

MAD2L1 binding protein; CMT2, KIAA0110, MGC11282, RP1-261G23.6; OTTHUMP00000016496; caught by MAD2 protein; KIAA0110; dJ261G23.1

UniProt ID

Q15013

GeneID

9587

Chromosome  Location

6p21.1

Function

protein binding

Reference

Yang, M.,  Li, B.,  Tomchick, D.R.,  Machius, M.,  Rizo, J.,  Yu, H.,  Luo, X. p31comet blocks Mad2 activation through structural mimicry.Cell(Cambridge,Mass.)2007; 131: 744-755