[NMR paper] NMR structural studies of domain 1 of receptor-associated protein.

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NMR structural studies of domain 1 of receptor-associated protein.

Related Articles NMR structural studies of domain 1 of receptor-associated protein.

J Biomol NMR. 2004 Jul;29(3):271-9

Authors: Wu Y, Migliorini M, Walsh J, Yu P, Strickland DK, Wang YX

The 39 kDa receptor-associated protein (RAP) is an endoplasmic reticulum resident protein that binds tightly to the low-density lipoprotein receptor-related protein (LRP) as well as to other members of the low-density lipoprotein receptor superfamily. The association of RAP with LRP prevents this receptor from interacting with ligands. RAP is a three-domain protein that contains two independent LRP binding sites; one located within domains 1 and 2, and one located within domain 3. As the first step toward defining the structure of the full-length protein and understanding the interaction between RAP and this family of receptors, we have determined the 3D structure of domain 1 using constraints derived from heteronuclear multi-dimensional NMR spectra, including NOEs, dihedral angles, J-couplings and chemical shifts, as well as two sets of non-correlated residual dipolar couplings measured from the protein solutions in anisotropic media of Pf1 and 6% polyacrylamide gel. The backbone C(alpha) rmsd between the current structure and a homo-nuclear NOE-based structure is about 2 A. The large rmsd mainly reflects the significant differences in helical orientation and in the structural details of the long helix (helix 2) between the two structures.

PMID: 15213425 [PubMed - indexed for MEDLINE]



Source: PubMed