1I35

SOLUTION STRUCTURE OF THE RAS-BINDING DOMAIN OF THE PROTEIN KINASE BYR2 FROM SCHIZOSACCHAROMYCES POMBE

Summary for 1I35

• Entry DOI: 10.2210/pdb1i35/pdb
• Descriptor: PROTEIN KINASE BYR2 (1 entity in total)
• Functional Keywords: ubiquitin superfold, transferase
• Biological source: Schizosaccharomyces pombe (fission yeast)
• Total number of polymer chains: 1
• Total formula weight: 10987.69

Authors

Gronwald, W.,Huber, F.,Grunewald, P.,Sporner, M.,Wohlgemuth, S.,Herrmann, C.,Kalbitzer, H.R. (deposition date: 2001-02-13, release date: 2001-12-12, Last modification date: 2024-05-22)

Primary citation

Gronwald, W.,Huber, F.,Grunewald, P.,Sporner, M.,Wohlgemuth, S.,Herrmann, C.,Kalbitzer, H.R.
Solution structure of the Ras binding domain of the protein kinase Byr2 from Schizosaccharomyces pombe.
Structure, 9:1029-1041, 2001

PubMed Abstract: After activation, small GTPases such as Ras transfer the incoming signal to effectors by specifically interacting with the binding domain of these proteins. Structural details of the binding domain of different effectors determine which pathway is predominantly activated. Byr2 from fission yeast is a functional homolog of Raf, which is the direct downstream target of Ras in mammalians that initiates a protein kinase cascade. The amino acid sequence of Byr2's Ras binding domain is only weakly related to that of Raf, and Byr2's three-dimensional structure is unknown.

PubMed: 11709167
DOI: 10.1016/S0969-2126(01)00671-2

Experimental method

SOLUTION NMR