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1K8R

Crystal structure of Ras-Bry2RBD complex

Summary for 1K8R
Entry DOI10.2210/pdb1k8r/pdb
Related1C1Y 1HE8 1LFD
DescriptorTransforming protein P21/H-RAS-1, Protein kinase byr2, MAGNESIUM ION, ... (4 entities in total)
Functional Keywordssignal transduction, cancer, gtpase, ubiquitin fold, signaling protein
Biological sourceHomo sapiens (human)
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Cellular locationCell membrane; Lipid-anchor; Cytoplasmic side: P01112
Total number of polymer chains2
Total formula weight31847.96
Authors
Scheffzek, K.,Gruenewald, P.,Wohlgemuth, S.,Kabsch, W.,Tu, H.,Wigler, M.,Wittinghofer, A.,Herrmann, C. (deposition date: 2001-10-25, release date: 2002-03-13, Last modification date: 2023-08-16)
Primary citationScheffzek, K.,Grunewald, P.,Wohlgemuth, S.,Kabsch, W.,Tu, H.,Wigler, M.,Wittinghofer, A.,Herrmann, C.
The Ras-Byr2RBD complex: structural basis for Ras effector recognition in yeast.
Structure, 9:1043-1050, 2001
Cited by
PubMed Abstract: The small GTP binding protein Ras has important roles in cellular growth and differentiation. Mutant Ras is permanently active and contributes to cancer development. In its activated form, Ras interacts with effector proteins, frequently initiating a kinase cascade. In the lower eukaryotic Schizosaccharomyces pombe, Byr2 kinase represents a Ras target that in terms of signal-transduction hierarchy can be considered a homolog of mammalian Raf-kinase. The activation mechanism of protein kinases by Ras is not understood, and there is no detailed structural information about Ras binding domains (RBDs) in nonmammalian organisms.
PubMed: 11709168
DOI: 10.1016/S0969-2126(01)00674-8
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (3 Å)
Structure validation

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