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). Publishing Authors By Initials
The structure of receptor-associated protein (RAP). Journal Published:
PUBLICATION TYPE: Research Support, N.I.H., Intr
Journal: Protein science : a publication of the Protein Soc
VOLUME: 16
Page Numbers: 1628-40
Journal Abbreviation: Protein Sci.
ISSN: 0961-8368
DAY: 3
MONTH: Aug
YEAR: 2007
The structure of receptor-associated protein (RAP). Information
Number of References:
LANGUAGE: eng
NlmUniqueID: 9211750
The structure of receptor-associated protein (RAP). Keywords Mesh Terms:
KEYWORDS: Scattering, Small Angle
MESH TERMS: chemistry
Chemical & Substance for Abstract: The structure of receptor-associated protein (RAP). Information
Substance Name: LDL-Receptor Related Protein-Associated
Registry Number: 0
Grant and Affiliation Information for The structure of receptor-associated protein (RAP).
AFFILIATION: Protein-Nucleic Acid Interaction Section, Structural Biophysics Laboratory, National Cancer Institute at Frederick, National Institutes of Health, Frederick, Maryland 21702, USA.
Country: United States
AGENCY: United States NCI
GRANT: N01-CO56000
ACRONYM: CO
MEDLINETA: Protein Sci
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