Abstract
The X-ray crystal structure of the complex between the Ras-related protein Rap1A in the GTP-analogue (GppNHp) form and the Ras-binding domain (RBD) of the Ras effector molecule c-Raf1, a Ser/Thr-specific protein kinase, has been solved to a resolution of 2.2 A. It shows that RBD has the ubiquitin superfold and that the structure of Rap1A is very similar to that of Ras. The interaction between the two proteins is mediated by an apparent central antiparallel beta-sheet formed by strands B1-B2 from RBD and strands beta 2-beta 3 from Rap1A. Complex formation is mediated by main-chain and side-chain interactions of the so-called effector residues in the switch I region of Rap1A.
MeSH terms
-
Amino Acid Sequence
-
Animals
-
Binding Sites
-
Computer Graphics
-
Crystallography, X-Ray
-
Escherichia coli
-
GTP Phosphohydrolases / metabolism
-
GTP-Binding Proteins / chemistry*
-
GTP-Binding Proteins / metabolism
-
Guanylyl Imidodiphosphate / chemistry*
-
Guanylyl Imidodiphosphate / metabolism
-
Humans
-
Molecular Sequence Data
-
Protein Conformation
-
Protein Serine-Threonine Kinases / chemistry*
-
Protein Serine-Threonine Kinases / metabolism
-
Proto-Oncogene Proteins / chemistry*
-
Proto-Oncogene Proteins / metabolism
-
Proto-Oncogene Proteins c-raf
-
Recombinant Proteins / chemistry
-
Recombinant Proteins / metabolism
-
Signal Transduction
-
rap GTP-Binding Proteins
Substances
-
Proto-Oncogene Proteins
-
Recombinant Proteins
-
Guanylyl Imidodiphosphate
-
Protein Serine-Threonine Kinases
-
Proto-Oncogene Proteins c-raf
-
GTP Phosphohydrolases
-
GTP-Binding Proteins
-
rap GTP-Binding Proteins