1c1y: Difference between revisions

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[[Image:1c1y.gif|left|200px]]<br /><applet load="1c1y" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:1c1y.gif|left|200px]]
caption="1c1y, resolution 1.90&Aring;" />
 
'''CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).'''<br />
{{Structure
|PDB= 1c1y |SIZE=350|CAPTION= <scene name='initialview01'>1c1y</scene>, resolution 1.90&Aring;
|SITE=
|LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=GTP:GUANOSINE-5'-TRIPHOSPHATE'>GTP</scene>
|ACTIVITY=
|GENE=
}}
 
'''CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
1C1Y is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MG:'>MG</scene>, <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=GTP:'>GTP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C1Y OCA].  
1C1Y is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1C1Y OCA].  


==Reference==
==Reference==
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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=7791872 7791872]
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:[http://www.ncbi.nlm.nih.gov/pubmed/7791872 7791872]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: GTP]]
[[Category: GTP]]
[[Category: MG]]
[[Category: MG]]
[[Category: effectors]]
[[Category: effector]]
[[Category: gtp-binding proteins]]
[[Category: gtp-binding protein]]
[[Category: protein-protein complex]]
[[Category: protein-protein complex]]


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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:18:46 2008''

Revision as of 11:18, 20 March 2008

File:1c1y.gif


PDB ID 1c1y

Drag the structure with the mouse to rotate
, resolution 1.90Å
Ligands: , and
Coordinates: save as pdb, mmCIF, xml



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


OverviewOverview

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.

DiseaseDisease

Known diseases associated with this structure: LEOPARD syndrome 2 OMIM:[164760], Noonan syndrome 5 OMIM:[164760]

About this StructureAbout this Structure

1C1Y is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

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

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