1C1Y

CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).

Summary for 1C1Y

• Entry DOI: 10.2210/pdb1c1y/pdb
• Related: 1GUA
• Descriptor: RAS-RELATED PROTEIN RAP-1A, PROTO-ONCOGENE SERINE/THREONINE PROTEIN KINASE RAF-1, MAGNESIUM ION, ... (6 entities in total)
• Functional Keywords: gtp-binding proteins, protein-protein complex, effectors, signaling protein
• Biological source: Homo sapiens (human); More
• Cellular location: Cell membrane; Lipid-anchor: P62834; Cytoplasm (By similarity): P04049
• Total number of polymer chains: 2
• Total formula weight: 28432.49

Authors

Nassar, N. (deposition date: 1999-07-22, release date: 1999-08-02, Last modification date: 2024-02-07)

Primary citation

Nassar, N.
The 2.2 A crystal structure of the Ras-binding domain of the serine/threonine kinase c-Raf1 in complex with Rap1A and a GTP analogue.
Nature, 375:554-560, 1995

PubMed 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.

PubMed: 7791872
DOI: 10.1038/375554a0

Experimental method

X-RAY DIFFRACTION (1.9 Å)