2mbg: Difference between revisions
From Proteopedia
Jump to navigationJump to search
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
{{Large structure}} | |||
{{STRUCTURE_2mbg| PDB=2mbg | SCENE= }} | |||
===Rlip76 (gap-gbd)=== | |||
{{ABSTRACT_PUBMED_24207123}} | |||
==Function== | |||
[[http://www.uniprot.org/uniprot/RBP1_HUMAN RBP1_HUMAN]] Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin.<ref>PMID:7673236</ref> <ref>PMID:12775724</ref> <ref>PMID:11437348</ref> | |||
==About this Structure== | |||
[[2mbg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBG OCA]. | |||
==Reference== | |||
<ref group="xtra">PMID:024207123</ref><references group="xtra"/><references/> | |||
[[Category: Campbell, L J.]] | |||
[[Category: Mott, H R.]] | |||
[[Category: Nietlispach, D.]] | |||
[[Category: Owen, D.]] | |||
[[Category: Rajasekar, K V.]] | |||
[[Category: Protein binding]] | |||
[[Category: Ralbp1]] | |||
[[Category: Rhogap]] | |||
Revision as of 07:24, 4 December 2013
Warning: this is a large structure, and loading might take a long time or not happen at all.
Rlip76 (gap-gbd)
Template:ABSTRACT PUBMED 24207123
Function
[RBP1_HUMAN] Can activate specifically hydrolysis of GTP bound to RAC1 and CDC42, but not RALA. Mediates ATP-dependent transport of S-(2,4-dinitrophenyl)-glutathione (DNP-SG) and doxorubicin (DOX) and is the major ATP-dependent transporter of glutathione conjugates of electrophiles (GS-E) and DOX in erythrocytes. Can catalyze transport of glutathione conjugates and xenobiotics, and may contribute to the multidrug resistance phenomenon. Serves as a scaffold protein that brings together proteins forming an endocytotic complex during interphase and also with CDK1 to switch off endocytosis, One of its substrates would be EPN1/Epsin.[1] [2] [3]
About this Structure
2mbg is a 1 chain structure. Full experimental information is available from OCA.
Reference
- Rajasekar KV, Campbell LJ, Nietlispach D, Owen D, Mott HR. The Structure of the RLIP76 RhoGAP-Ral Binding Domain Dyad: Fixed Position of the Domains Leads to Dual Engagement of Small G Proteins at the Membrane. Structure. 2013 Oct 22. pii: S0969-2126(13)00357-2. doi:, 10.1016/j.str.2013.09.007. PMID:24207123 doi:https://dx.doi.org/10.1016/j.str.2013.09.007
- ↑ Jullien-Flores V, Dorseuil O, Romero F, Letourneur F, Saragosti S, Berger R, Tavitian A, Gacon G, Camonis JH. Bridging Ral GTPase to Rho pathways. RLIP76, a Ral effector with CDC42/Rac GTPase-activating protein activity. J Biol Chem. 1995 Sep 22;270(38):22473-7. PMID:7673236
- ↑ Rosse C, L'Hoste S, Offner N, Picard A, Camonis J. RLIP, an effector of the Ral GTPases, is a platform for Cdk1 to phosphorylate epsin during the switch off of endocytosis in mitosis. J Biol Chem. 2003 Aug 15;278(33):30597-604. Epub 2003 May 29. PMID:12775724 doi:https://dx.doi.org/10.1074/jbc.M302191200
- ↑ Sharma R, Singhal SS, Cheng J, Yang Y, Sharma A, Zimniak P, Awasthi S, Awasthi YC. RLIP76 is the major ATP-dependent transporter of glutathione-conjugates and doxorubicin in human erythrocytes. Arch Biochem Biophys. 2001 Jul 15;391(2):171-9. PMID:11437348 doi:https://dx.doi.org/10.1006/abbi.2001.2395
