Table 1 Sequence conservation of selected residues that mediate trimeric complex formation

From: Cryo-EM structure of the CDK2-cyclin A-CDC25A complex

CDK2

CDK1

CDK3

CDK4

CDK6

 

Glu12

Glu

Glu

Val

Glu

 

Glu42

Glu

Glu

Gly

Glu

 

Gln131

Gln

Gln

Glu

Gln

 

Glu162

Glu

Glu

Val

Val

 

Asp206

Asp

Asp

Asn

Ser

 

Glu208

Glu

Glu

Glu

Asp

 

Asp210

Asp

Asp

Asp

Asp

 

Phe213

Phe

Phe

Gly

Gly

 

Arg217

Arg

Arg

Asp

Asp

 

9 residues

9 conserved

9 conserved

2 conserved

4 conserved

 

cyclin A (bovine)

cyclin A (human)

cyclin B (human)

cyclin E (human)

cyclin D1 (human)

cyclin D3 (human)

Tyr269

Tyr

Tyr

Tyr

Ile

Thr

Glu272

Glu

Glu

Lys

Thr

Thr

2 residues

2 conserved

2 conserved

1 conserved

0 conserved

0 conserved

CDC25A

CDC25B

CDC25C

   

Lys353

Lys

Lys

   

Gln355

Gln

Gln

   

Ser435

Ser

Ser

   

Arg446

Arg

Arg

   

Glu447

Glu

Glu

   

Arg450

Arg

Arg

   

Tyr455

Tyr

Tyr

   

Arg506

Arg

Lys

   

Ser513

Ser

Gln

   

Lys514

Arg

Leu

   

10 residues

9 conserved

7 conserved

   
  1. Selected residues of (a) CDK2 (b) cyclin A and (c) CDC25A identified from the cryo-EM structure that mediate complex formation. The number of conserved residues across relevant CDKs, cyclins and CDC25 isoforms is indicated. Complete sequence alignments are provided in Supplementary Fig. 7.
Back to article page