2byf: Difference between revisions
New page: left|200px<br /><applet load="2byf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2byf" /> '''NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EP... |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:2byf.gif|left|200px]]<br /><applet load="2byf" size=" | [[Image:2byf.gif|left|200px]]<br /><applet load="2byf" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="2byf" /> | caption="2byf" /> | ||
'''NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EPSILON RA 2 DOMAIN'''<br /> | '''NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EPSILON RA 2 DOMAIN'''<br /> | ||
==Overview== | ==Overview== | ||
Ras proteins signal to a number of distinct pathways by interacting with | 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. | ||
==About this Structure== | ==About this Structure== | ||
2BYF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 2BYF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence 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=2BYF OCA]. | ||
==Reference== | ==Reference== | ||
| Line 13: | Line 13: | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Bunney, T | [[Category: Bunney, T D.]] | ||
[[Category: Driscoll, P | [[Category: Driscoll, P C.]] | ||
[[Category: Esposito, D.]] | [[Category: Esposito, D.]] | ||
[[Category: Gandarillas, N | [[Category: Gandarillas, N L.]] | ||
[[Category: Gieschik, P.]] | [[Category: Gieschik, P.]] | ||
[[Category: Harris, R.]] | [[Category: Harris, R.]] | ||
[[Category: Josephs, M | [[Category: Josephs, M B.]] | ||
[[Category: Katan, M.]] | [[Category: Katan, M.]] | ||
[[Category: Paterson, H | [[Category: Paterson, H F.]] | ||
[[Category: Pearl, L | [[Category: Pearl, L H.]] | ||
[[Category: Rodrigues-Lima, F.]] | [[Category: Rodrigues-Lima, F.]] | ||
[[Category: Roe, S | [[Category: Roe, S M.]] | ||
[[Category: lipase]] | [[Category: lipase]] | ||
[[Category: phospholipase c epsilon]] | [[Category: phospholipase c epsilon]] | ||
| Line 30: | Line 30: | ||
[[Category: ubiquitin superfold]] | [[Category: ubiquitin superfold]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:43:00 2008'' | ||
Revision as of 14:43, 21 February 2008
|
NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EPSILON RA 2 DOMAIN
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.
About this Structure
2BYF is a Single protein structure of sequence 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 Thu Feb 21 16:43:00 2008
