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The structure of receptor-associated protein (RAP)

  1. Author:
    Lee, D.
    Walsh, J. D.
    Migliorini, M.
    Yu, P.
    Cai, T.
    Schwieters, C. D.
    Krueger, S.
    Strickl, D. K.
    Wang, Y. X.

  2. Author Address

    NCI, Natl Inst Hlth, Struct Biophys Lab, Nucl Acid Interact Sect, Frederick, MD 21702 USA. Univ Maryland, Sch Med, Ctr Vasc & Inflam Dis, Dept Surg & Physiol, Baltimore, MD 21201 USA. NCI, SAIC Frederick Inc, Basic Res Program, Frederick, MD 21702 USA. NIDCR, Natl Inst Hlth, Expt Med Sect, Bethesda, MD 20892 USA. Natl Inst Hlth, Ctr Informat Technol, Div Computat Biosci, Bethesda, MD 20892 USA. NIST, Ctr Neutron Res, Natl Inst Stand & Technol, Gaithersburg, MD 20899 USA.;Wang, YX, NCI, Natl Inst Hlth, Struct Biophys Lab, Nucl Acid Interact Sect, Frederick, MD 21702 USA.;wangyu@ncifcrf.gov
    1. Year: 2007
    2. Date: Aug
  2. Journal: Protein Science
    1. 16
    2. 8
    3. Pages: 1628-1640
  4. Type of Article: Article
  5. ISSN: 0961-8368
  1. Abstract:

    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.

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External Sources

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  2. DOI: 10.1110/ps.072865407
  3. View record in Web of Science®
  4. WOS: 000248360600012

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