Proteomics

Dataset Information

0

CXMS BS3 Ras/BRAF/MEK/1433 complex


ABSTRACT: RAF-family kinases are activated by recruitment to the plasma membrane by GTP-bound RAS, where they initiate signaling through the MAP kinase cascade. Here we crosslinked (BS3), digested (trypsin), and analyzed via LC-MS/MS KRAS (human, residues 1-169) bound to intact BRAF (human) in an autoinhibited state with MEK1 (human, ) and a 14-3-3 (SF9) dimer . Analysis of this KRAS/BRAF/MEK1/14-3-3 complex reveals both interprotein and intraprotein crosslinks.

INSTRUMENT(S): Orbitrap Eclipse

ORGANISM(S): Homo Sapiens (human) Spodoptera Frugiperda

SUBMITTER: Anna Schmoker  

LAB HEAD: Michael Eck

PROVIDER: PXD042584 | Pride | 2023-10-24

REPOSITORIES: Pride

Dataset's files

Source:
Action DRS
KRAS-BRAF-MEK-1433_sequences.fasta Fasta
ams_00252.mgf Mgf
ams_00252.raw Raw
ams_00252_ProteinProspector_cross-linked_spectra.txt Txt
ams_00252_pLink2_cross-linked_spectra.csv Csv
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Publications

Cryo-EM structure of a RAS/RAF recruitment complex.

Park Eunyoung E   Rawson Shaun S   Schmoker Anna A   Kim Byeong-Won BW   Oh Sehee S   Song Kangkang K   Jeon Hyesung H   Eck Michael J MJ  

Nature communications 20230729 1


RAF-family kinases are activated by recruitment to the plasma membrane by GTP-bound RAS, whereupon they initiate signaling through the MAP kinase cascade. Prior structural studies of KRAS with RAF have focused on the isolated RAS-binding and cysteine-rich domains of RAF (RBD and CRD, respectively), which interact directly with RAS. Here we describe cryo-EM structures of a KRAS bound to intact BRAF in an autoinhibited state with MEK1 and a 14-3-3 dimer. Analysis of this KRAS/BRAF/MEK1/14-3-3 comp  ...[more]

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