Irina Mikhailenko

Publication Detail

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Dissection of RAP-LRP interactions: binding of RAP and RAP fragments to complement-like repeats 7 and 8 from ligand binding cluster II of LRP.

Ana Lazic; Klavs Dolmer; Dudley K Strickland; Peter G W Gettins (Profiled Author: Dudley K Strickland)

Department of Biochemistry and Molecular Genetics, College of Medicine, University of Illinois at Chicago, Chicago, IL 60607, USA.
Archives of biochemistry and biophysics 2006;450(2):167-75.

The receptor associated protein (RAP) is a three domain 38kDa ER-resident chaperone that helps folding of LRP and other LDL receptor family members and prevents premature binding of protein ligands. It competes strongly with all known LRP ligands. To further understanding of the specificity of RAP-LRP interactions, the binding of RAP and RAP fragments to two domains (CR7-CR8) from one of the main ligand-binding regions of LRP has been examined by 2D HSQC NMR spectroscopy and isothermal titration calorimetry. We found that RAP contains two binding sites for CR7-CR8, with the higher affinity site (K(d) approximately 1microM) located in the C-terminal two-thirds and the weaker site (K(d) approximately 5microM) in the N-terminal third of RAP. Residues from both CR7 and CR8 are involved in binding at each RAP site. The presence of more than one binding site on RAP for CR domains from LRP, together with the previous demonstration by others that RAP can bind to CR5-CR6 with comparably low affinities suggest an explanation for the dual roles of RAP as a folding chaperone and a tight competitive inhibitor of ligand binding.

2 Originating Grant

• 1.

  MEDVED, LEONID V.

  Fibrin(ogen) Structure and Interactions

  1 January 1998 - 31 July 2012

  NATIONAL HEART, LUNG, AND BLOOD INSTITUTE

• 2.

  STRICKLAND, DUDLEY K.

  Regulation of Surface Receptors by LRP

  30 September 1993 - 30 June 2012

  NATIONAL HEART, LUNG, AND BLOOD INSTITUTE

Scientific Context

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