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1c1y

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1c1y, resolution 1.90Å ()

Sites:

, and

Ligands:

, ,

Related:

1gua

Structural annotation:
Resources:	CATH : 1C1Ya00, 1C1Yb00 InterPro : Ipr001806, Ipr003577, Ipr005225, Ipr013753, Ipr000719, Ipr002219, Ipr003116, Ipr008271, Ipr011009, Ipr017441, Ipr017442 Pfam : PF00071, PF02196 SCOP : d1c1ya_, d1c1yb_ UniProt : P62834, P04049

Functional annotation:
Cellular component:	membrane plasma membrane cytosol intracellular mitochondrial outer membrane
Biological process:	signal transduction cell cycle intracellular signaling cascade negative regulation of cell cycle small GTPase mediated signal transduction nerve growth factor receptor signaling pathway Ras protein signal transduction protein amino acid phosphorylation cell proliferation apoptosis cytoskeleton organization and biogenesis
Molecular function:	GTPase activity nucleotide binding GTP binding protein binding protein serine/threonine kinase activity receptor signaling protein activity kinase activity protein kinase activity transferase activity metal ion binding ATP binding diacylglycerol binding zinc ion binding

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

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

Publication Abstract from PubMed

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.

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., Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A, Nature. 1995 Jun 15;375(6532):554-60. PMID:7791872

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

About this Structure

1c1y is a 2 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Nassar N, Horn G, Herrmann C, Scherer A, McCormick F, Wittinghofer A. 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. 1995 Jun 15;375(6532):554-60. PMID:7791872 doi:10.1038/375554a0
Rehmann H, Arias-Palomo E, Hadders MA, Schwede F, Llorca O, Bos JL. Structure of Epac2 in complex with a cyclic AMP analogue and RAP1B. Nature. 2008 Sep 4;455(7209):124-7. Epub 2008 Jul 27. PMID:18660803 doi:10.1038/nature07187

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1c1y

From Proteopedia

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

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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