1c1y: Difference between revisions
New page: left|200px<br /> <applet load="1c1y" size="450" color="white" frame="true" align="right" spinBox="true" caption="1c1y, resolution 1.90Å" /> '''CRYSTAL STRUCTURE O... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1c1y.gif|left|200px]]<br /> | [[Image:1c1y.gif|left|200px]]<br /><applet load="1c1y" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="1c1y" size=" | |||
caption="1c1y, resolution 1.90Å" /> | caption="1c1y, resolution 1.90Å" /> | ||
'''CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).'''<br /> | '''CRYSTAL STRUCTURE OF RAP.GMPPNP IN COMPLEX WITH THE RAS-BINDING-DOMAIN OF C-RAF1 KINASE (RAFRBD).'''<br /> | ||
==Overview== | ==Overview== | ||
The X-ray crystal structure of the complex between the Ras-related protein | 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. | ||
==Disease== | |||
Known diseases associated with this structure: LEOPARD syndrome 2 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=164760 164760]], Noonan syndrome 5 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=164760 164760]] | |||
==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 MG, CA and GTP as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | 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]. | ||
==Reference== | ==Reference== | ||
| Line 22: | Line 24: | ||
[[Category: protein-protein complex]] | [[Category: protein-protein complex]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:01:30 2008'' | ||
Revision as of 13:01, 21 February 2008
|
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 with , and as ligands. 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
Page seeded by OCA on Thu Feb 21 12:01:30 2008