2mbg

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'''Unreleased structure'''
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{{Large structure}}
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{{STRUCTURE_2mbg| PDB=2mbg | SCENE= }}
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===Rlip76 (gap-gbd)===
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{{ABSTRACT_PUBMED_24207123}}
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The entry 2mbg is ON HOLD until Paper Publication
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==Function==
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[[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>
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Authors: Rajasekar, K.V., Campbell, L.J., Nietlispach, D., Owen, D., Mott, H.R.
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==About this Structure==
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[[2mbg]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBG OCA].
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Description: Rlip76 (gap-gbd)
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==Reference==
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<ref group="xtra">PMID:024207123</ref><references group="xtra"/><references/>
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[[Category: Campbell, L J.]]
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[[Category: Mott, H R.]]
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[[Category: Nietlispach, D.]]
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[[Category: Owen, D.]]
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[[Category: Rajasekar, K V.]]
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[[Category: Protein binding]]
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[[Category: Ralbp1]]
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[[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.

Template:STRUCTURE 2mbg

Contents

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:http://dx.doi.org/10.1016/j.str.2013.09.007
  1. ↑ 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
  2. ↑ 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:http://dx.doi.org/10.1074/jbc.M302191200
  3. ↑ 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:http://dx.doi.org/10.1006/abbi.2001.2395

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