1K8R
Crystal structure of Ras-Bry2RBD complex
Summary for 1K8R
Entry DOI | 10.2210/pdb1k8r/pdb |
Related | 1C1Y 1HE8 1LFD |
Descriptor | Transforming protein P21/H-RAS-1, Protein kinase byr2, MAGNESIUM ION, ... (4 entities in total) |
Functional Keywords | signal transduction, cancer, gtpase, ubiquitin fold, signaling protein |
Biological source | Homo sapiens (human) More |
Cellular location | Cell membrane; Lipid-anchor; Cytoplasmic side: P01112 |
Total number of polymer chains | 2 |
Total formula weight | 31847.96 |
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 citation | Scheffzek, 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: 11709168DOI: 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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