This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.
Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.
2byf
From Proteopedia
(New page: 200px<br /><applet load="2byf" size="450" color="white" frame="true" align="right" spinBox="true" caption="2byf" /> '''NMR SOLUTION STRUCTURE OF PHOSPHOLIPASE C EP...) |
|||
| 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
Categories: Homo sapiens | Single protein | Bunney, T D. | Driscoll, P C. | Esposito, D. | Gandarillas, N L. | Gieschik, P. | Harris, R. | Josephs, M B. | Katan, M. | Paterson, H F. | Pearl, L H. | Rodrigues-Lima, F. | Roe, S M. | Lipase | Phospholipase c epsilon | Ras binding domain | Ubiquitin superfold
