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2mbg
From Proteopedia
(Difference between revisions)
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==Rlip76 (gap-gbd)== | ==Rlip76 (gap-gbd)== | ||
| - | <StructureSection load='2mbg' size='340' side='right' caption='[[2mbg]], [[NMR_Ensembles_of_Models | 35 NMR models]]' scene=''> | + | <StructureSection load='2mbg' size='340' side='right'caption='[[2mbg]], [[NMR_Ensembles_of_Models | 35 NMR models]]' scene=''> |
== Structural highlights == | == Structural highlights == | ||
| - | <table><tr><td colspan='2'>[[2mbg]] is a 1 chain structure with sequence from [ | + | <table><tr><td colspan='2'>[[2mbg]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2MBG OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2MBG FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RALBP1, RLIP1, RLIP76 ([ | + | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RALBP1, RLIP1, RLIP76 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[ | + | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2mbg FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2mbg OCA], [https://pdbe.org/2mbg PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2mbg RCSB], [https://www.ebi.ac.uk/pdbsum/2mbg PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2mbg ProSAT]</span></td></tr> |
</table> | </table> | ||
| - | {{Large structure}} | ||
== Function == | == Function == | ||
| - | [[ | + | [[https://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> |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</StructureSection> | </StructureSection> | ||
[[Category: Human]] | [[Category: Human]] | ||
| + | [[Category: Large Structures]] | ||
[[Category: Campbell, L J]] | [[Category: Campbell, L J]] | ||
[[Category: Mott, H R]] | [[Category: Mott, H R]] | ||
Revision as of 10:06, 26 May 2021
Rlip76 (gap-gbd)
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Categories: Human | Large Structures | Campbell, L J | Mott, H R | Nietlispach, D | Owen, D | Rajasekar, K V | Protein binding | Ralbp1 | Rhogap
