We apologize for Proteopedia being slow to respond. For the past two years, a new implementation of Proteopedia has been being built. Soon, it will replace this 18-year old system. All existing content will be moved to the new system at a date that will be announced here.

2ftu

From Proteopedia

(Difference between revisions)

Jump to: navigation, search

Current revision

solution structure of domain 3 of RAP

Structural highlights

2ftu is a 1 chain structure with sequence from Homo sapiens. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Disease

AMRP_HUMAN Note=In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.

Function

AMRP_HUMAN Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

The receptor associated protein (RAP) is an antagonist and molecular chaperone that binds tightly to low-density lipoprotein receptor family members in the endoplasmic reticulum (ER). After escorting these receptors to the Golgi, RAP dissociates from the receptors. The molecular mechanism of the dissociation has been unknown until now. The solution structure of RAP-D3 domain presented here reveals a striking increase in positively charged residues on the surface of this RAP domain due to protonation of solvent-exposed histidine sidechains as the pH is reduced from a near neutral pH of the ER to the acidic pH of the Golgi. Structure-based mutagenesis studies in vitro and in cells confirm that the protonation of histidine residues as a consequence of the pH changes modulate the binding/release of RAP from LRP. This histidine switch may serve as a general mechanism for regulating cell trafficking events.

RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi.,Lee D, Walsh JD, Mikhailenko I, Yu P, Migliorini M, Wu Y, Krueger S, Curtis JE, Harris B, Lockett S, Blacklow SC, Strickland DK, Wang YX Mol Cell. 2006 May 5;22(3):423-30. PMID:16678114^[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Lee D, Walsh JD, Mikhailenko I, Yu P, Migliorini M, Wu Y, Krueger S, Curtis JE, Harris B, Lockett S, Blacklow SC, Strickland DK, Wang YX. RAP uses a histidine switch to regulate its interaction with LRP in the ER and Golgi. Mol Cell. 2006 May 5;22(3):423-30. PMID:16678114 doi:10.1016/j.molcel.2006.04.011

1 Structural highlights
2 Disease
3 Function
4 Evolutionary Conservation
5 Publication Abstract from PubMed
6 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2ftu"

Categories: Homo sapiens | Large Structures | Lee D | Walsh JD | Wang Y-X

@@ Line 1: / Line 1: @@
 ==solution structure of domain 3 of RAP==
-<StructureSection load='2ftu' size='340' side='right'caption='[[2ftu]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2ftu' size='340' side='right'caption='[[2ftu]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2ftu]] 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=2FTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FTU FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2ftu]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2FTU OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2FTU FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2fft|2fft]], [[2ffv|2ffv]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
-<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">LRPAP1 ([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'>[https://proteopedia.org/fgij/fg.htm?mol=2ftu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ftu OCA], [https://pdbe.org/2ftu PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ftu RCSB], [https://www.ebi.ac.uk/pdbsum/2ftu PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ftu ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[https://www.uniprot.org/uniprot/AMRP_HUMAN AMRP_HUMAN]] Note=In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.
+[https://www.uniprot.org/uniprot/AMRP_HUMAN AMRP_HUMAN] Note=In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.
 == Function ==
-[[https://www.uniprot.org/uniprot/AMRP_HUMAN AMRP_HUMAN]] Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.
+[https://www.uniprot.org/uniprot/AMRP_HUMAN AMRP_HUMAN] Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 35: / Line 34: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Lee, D]]
+[[Category: Lee D]]
-[[Category: Walsh, J D]]
+[[Category: Walsh JD]]
-[[Category: Wang, Y X]]
+[[Category: Wang Y-X]]
-[[Category: Domain 3]]
-[[Category: Lipid binding protein]]
-[[Category: Rap]]
-[[Category: Receptor-associated protein]]

2ftu

From Proteopedia

Current revision

solution structure of domain 3 of RAP

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox