2P01

The structure of receptor-associated protein(RAP)

Summary for 2P01

• Entry DOI: 10.2210/pdb2p01/pdb
• Related: 2P03
• Descriptor: Alpha-2-macroglobulin receptor-associated protein (1 entity in total)
• Functional Keywords: receptor-associated protein, rap, cell adhesion
• Biological source: Homo sapiens (human)
• Cellular location: Endoplasmic reticulum: P30533
• Total number of polymer chains: 1
• Total formula weight: 37849.60

Authors

Lee, D.,Walsh, J.D.,Migliorini, M.,Yu, P.,Cai, T.,Schwieters, C.D.,Krueger, S.,Strickland, D.K.,Wang, Y.X. (deposition date: 2007-02-28, release date: 2007-08-21, Last modification date: 2024-05-22)

Primary citation

Lee, D.,Walsh, J.D.,Migliorini, M.,Yu, P.,Cai, T.,Schwieters, C.D.,Krueger, S.,Strickland, D.K.,Wang, Y.X.
The structure of receptor-associated protein (RAP).
Protein Sci., 16:1628-1640, 2007

PubMed 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.

PubMed: 17656581
DOI: 10.1110/ps.072865407

Experimental method

SOLUTION NMR