2c5l
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 2c5l |SIZE=350|CAPTION= <scene name='initialview01'>2c5l</scene>, resolution 1.90Å | |PDB= 2c5l |SIZE=350|CAPTION= <scene name='initialview01'>2c5l</scene>, resolution 1.90Å | ||
|SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+C'>AC1</scene> | |SITE= <scene name='pdbsite=AC1:Gol+Binding+Site+For+Chain+C'>AC1</scene> | ||
| - | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GTP:GUANOSINE-5 | + | |LIGAND= <scene name='pdbligand=MG:MAGNESIUM+ION'>MG</scene>, <scene name='pdbligand=GTP:GUANOSINE-5'-TRIPHOSPHATE'>GTP</scene> and <scene name='pdbligand=GOL:GLYCEROL'>GOL</scene> |
|ACTIVITY= [http://en.wikipedia.org/wiki/Small_monomeric_GTPase Small monomeric GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.2 3.6.5.2] | |ACTIVITY= [http://en.wikipedia.org/wiki/Small_monomeric_GTPase Small monomeric GTPase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.6.5.2 3.6.5.2] | ||
|GENE= | |GENE= | ||
| Line 45: | Line 45: | ||
[[Category: ubiquitin superfold]] | [[Category: ubiquitin superfold]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 23 14:50:26 2008'' |
Revision as of 12:50, 23 March 2008
| |||||||
| , resolution 1.90Å | |||||||
|---|---|---|---|---|---|---|---|
| Sites: | |||||||
| Ligands: | , and | ||||||
| Activity: | Small monomeric GTPase, with EC number 3.6.5.2 | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF PLC EPSILON RAS ASSOCIATION DOMAIN WITH HRAS
Contents |
Overview
Ras proteins signal to a number of distinct pathways by interacting with diverse effectors. Studies of ras/effector interactions have focused on three classes, Raf kinases, ral guanylnucleotide-exchange factors, and phosphatidylinositol-3-kinases. Here we describe ras interactions with another effector, the recently identified phospholipase C epsilon (PLCepsilon). We solved structures of PLCepsilon RA domains (RA1 and RA2) by NMR and the structure of the RA2/ras complex by X-ray crystallography. Although the similarity between ubiquitin-like folds of RA1 and RA2 proves that they are homologs, only RA2 can bind ras. Some of the features of the RA2/ras interface are unique to PLCepsilon, while the ability to make contacts with both switch I and II regions of ras is shared only with phosphatidylinositol-3-kinase. Studies of PLCepsilon regulation suggest that, in a cellular context, the RA2 domain, in a mode specific to PLCepsilon, has a role in membrane targeting with further regulatory impact on PLC activity.
Disease
Known diseases associated with this structure: Bladder cancer, somatic OMIM:[190020], Costello syndrome OMIM:[190020], Thyroid carcinoma, follicular, somatic OMIM:[190020]
About this Structure
2C5L is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Structural and mechanistic insights into ras association domains of phospholipase C epsilon., Bunney TD, Harris R, Gandarillas NL, Josephs MB, Roe SM, Sorli SC, Paterson HF, Rodrigues-Lima F, Esposito D, Ponting CP, Gierschik P, Pearl LH, Driscoll PC, Katan M, Mol Cell. 2006 Feb 17;21(4):495-507. PMID:16483931
Page seeded by OCA on Sun Mar 23 14:50:26 2008
Categories: Homo sapiens | Protein complex | Small monomeric GTPase | Bunney, T D. | Katan, M. | Pearl, L H. | Roe, S M. | GOL | GTP | MG | Disease mutation | Gtp-binding | Lipoprotein | Nucleotide-binding | Oncogene | Palmitate | Prenylation | Proto-oncogene | Ra | Signaling protein | Ubiquitin superfold
