2p01 | pdb_00002p01

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The structure of receptor-associated protein(RAP)

File:2p01.gif


2p01

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Overview

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.

About this Structure

2P01 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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

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