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2p01

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Current revision

The structure of receptor-associated protein(RAP)

Structural highlights

2p01 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 a molecular chaperone that binds tightly to certain newly synthesized LDL receptor family members in the endoplasmic reticulum (ER) and facilitates their delivery to the Golgi. We have adopted a divide-and-conquer strategy to solve the structures of the individual domains of RAP using NMR spectroscopy. We present here the newly determined structure of domain 2. Based on this structure and the structures of domains 1 and 3, which were solved previously, we utilized experimental small-angle neutron scattering (SANS) data and a novel simulated annealing protocol to characterize the overall structure of RAP. The results reveal that RAP adopts a unique structural architecture consisting of three independent three-helix bundles that are connected by long and flexible linkers. The flexible linkers and the quasi-repetitive structural architecture may allow RAP to adopt various possible conformations when interacting with the LDL receptors, which are also made of repetitive substructure units.

The structure of receptor-associated protein (RAP).,Lee D, Walsh JD, Migliorini M, Yu P, Cai T, Schwieters CD, Krueger S, Strickland DK, Wang YX Protein Sci. 2007 Aug;16(8):1628-40. PMID:17656581^[1]

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

References

↑ Lee D, Walsh JD, Migliorini M, Yu P, Cai T, Schwieters CD, Krueger S, Strickland DK, Wang YX. The structure of receptor-associated protein (RAP). Protein Sci. 2007 Aug;16(8):1628-40. PMID:17656581 doi:16/8/1628

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/2p01"

@@ Line 1: / Line 1: @@
 ==The structure of receptor-associated protein(RAP)==
-<StructureSection load='2p01' size='340' side='right'caption='[[2p01]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='2p01' size='340' side='right'caption='[[2p01]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[2p01]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2P01 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=2P01 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[2p01]] 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=2P01 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2P01 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[2p03|2p03]]</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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=2p01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p01 OCA], [http://pdbe.org/2p01 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2p01 RCSB], [http://www.ebi.ac.uk/pdbsum/2p01 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2p01 ProSAT]</span></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=2p01 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2p01 OCA], [https://pdbe.org/2p01 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2p01 RCSB], [https://www.ebi.ac.uk/pdbsum/2p01 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2p01 ProSAT]</span></td></tr>
 </table>
 == Disease ==
-[[http://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 ==
-[[http://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 36: / Line 36: @@
 [[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Cai, T]]
+[[Category: Cai T]]
-[[Category: Krueger, S]]
+[[Category: Krueger S]]
-[[Category: Lee, D]]
+[[Category: Lee D]]
-[[Category: Migliorini, M]]
+[[Category: Migliorini M]]
-[[Category: Schwieters, C D]]
+[[Category: Schwieters CD]]
-[[Category: Strickland, D K]]
+[[Category: Strickland DK]]
-[[Category: Walsh, J D]]
+[[Category: Walsh JD]]
-[[Category: Wang, Y X]]
+[[Category: Wang YX]]
-[[Category: Yu, P]]
+[[Category: Yu P]]
-[[Category: Cell adhesion]]
-[[Category: Rap]]
-[[Category: Receptor-associated protein]]

2p01

From Proteopedia

Current revision

The structure of receptor-associated protein(RAP)

Structural highlights

Disease

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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