PDBsum entry 2p01

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protein links
Cell adhesion PDB id
Protein chain
323 a.a. *
* Residue conservation analysis
PDB id:
Name: Cell adhesion
Title: The structure of receptor-associated protein(rap)
Structure: Alpha-2-macroglobulin receptor-associated protein. Chain: a. Synonym: alpha-2- mrap, low density lipoprotein receptor- related protein-associated protein 1, rap
Source: Homo sapiens. Human. Organism_taxid: 9606
NMR struc: 20 models
Authors: D.Lee,J.D.Walsh,M.Migliorini,P.Yu,T.Cai,C.D.Schwieters, S.Krueger,D.K.Strickland,Y.X.Wang
Key ref:
D.Lee et al. (2007). The structure of receptor-associated protein (RAP). Protein Sci, 16, 1628-1640. PubMed id: 17656581 DOI: 10.1110/ps.072865407
28-Feb-07     Release date:   21-Aug-07    
Go to PROCHECK summary

Protein chain
Pfam   ArchSchema ?
P30533  (AMRP_HUMAN) -  Alpha-2-macroglobulin receptor-associated protein
357 a.a.
323 a.a.
Key:    PfamA domain  Secondary structure  CATH domain

 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     extracellular region   8 terms 
  Biological process     extracellular negative regulation of signal transduction   7 terms 
  Biochemical function     lipase binding     8 terms  


DOI no: 10.1110/ps.072865407 Protein Sci 16:1628-1640 (2007)
PubMed id: 17656581  
The structure of receptor-associated protein (RAP).
D.Lee, J.D.Walsh, M.Migliorini, P.Yu, T.Cai, C.D.Schwieters, S.Krueger, D.K.Strickland, Y.X.Wang.
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.
  Selected figure(s)  
Figure 3.
Figure 3. Binding of 125 I-labeled D1D2 WT and mutants to LRP
Figure 8.
Figure 8. Ribbon diagrams of the 10 lowest-energy SANS-refined in stereoview (A); two examples of the SANS-refined
  The above figures are reprinted by permission from the Protein Society: Protein Sci (2007, 16, 1628-1640) copyright 2007.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
20303980 M.Guttman, J.H.Prieto, T.M.Handel, P.J.Domaille, and E.A.Komives (2010).
Structure of the minimal interface between ApoE and LRP.
  J Mol Biol, 398, 306-319.
PDB codes: 2knx 2kny
19397492 J.K.Jensen, K.Dolmer, C.Schar, and P.G.Gettins (2009).
Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): consequences for the chaperone functions of RAP.
  Biochem J, 421, 273-282.  
19826010 T.Kanekiyo, and G.Bu (2009).
Receptor-associated protein interacts with amyloid-beta peptide and promotes its cellular uptake.
  J Biol Chem, 284, 33352-33359.  
19116273 X.V.Yang, Y.Banerjee, J.A.Fernández, H.Deguchi, X.Xu, L.O.Mosnier, R.T.Urbanus, Groot, T.C.White-Adams, O.J.McCarty, and J.H.Griffin (2009).
Activated protein C ligation of ApoER2 (LRP8) causes Dab1-dependent signaling in U937 cells.
  Proc Natl Acad Sci U S A, 106, 274-279.  
  18626063 A.P.Lillis, L.B.Van Duyn, J.E.Murphy-Ullrich, and D.K.Strickland (2008).
LDL receptor-related protein 1: unique tissue-specific functions revealed by selective gene knockout studies.
  Physiol Rev, 88, 887-918.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.