Table 1 MST measurement of binding affinity of KRAS to BRAF fragments and complexes

From: Cryo-EM structure of a RAS/RAF recruitment complex

BRAF construct/complex (residues)

Kd (nM)

Literature values (nM)

BRAF

CRAF*

BRAF RBD (151–232)

26.4 ± 13.9

11.2 (ref. 24)

21.2 (ref. 24)

356 (ref. 17)

BRAF BRS-RBD-CRD (39–320)

107.9 ± 60.1

64.6 (ref. 24)

190.5 (ref. 24)

152 (ref. 17)

BRAF BRS-RBD-CRD-C2 (39–434)

180.6 ± 123.6

 

188 (ref. 24)

BRAF CRD-kinase (233–766) with 14-3-3

ND

  

BRAF/14-3-3 (full length, active dimer)

105.5 ± 58.7

80.2 (ref. 24)†

 

BRAF/MEK/14-3-3 (autoinhibited)

127.3 ± 77.2

85/127 (ref. 7)‡

 
  1. *CRAF lacks a BRS domain; these studies measured binding to RBD or RBD-CRD constructs with SPR.
  2. †The activation state and 14-3-3 binding of the full-length BRAF in this study was not characterized.
  3. ‡Affinities were measured for binding of KRAS to autoinhibited BRAF complexes with and without MEK, respectively, using fluorescence polarization.
  4. Source data are provided in the Source Data File.
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