Quantitative Dissection of the Binding Contributions of Ligand Lysines of the Receptor-associated Protein (RAP) to the Low Density Lipoprotein Receptor-related Protein (LRP1)
Open Access
- 1 August 2013
- journal article
- Published by Elsevier BV
- Vol. 288 (33), 24081-24090
- https://doi.org/10.1074/jbc.m113.473728
Abstract
No abstract availableThis publication has 31 references indexed in Scilit:
- A proximal pair of positive charges provides the dominant ligand-binding contribution to complement-like domains from the LRP (low-density lipoprotein receptor-related protein)Biochemical Journal, 2012
- The Structure, Dynamics, and Binding of the LA45 Module Pair of the Low-Density Lipoprotein Receptor Suggest an Important Role for LA4 in Ligand ReleaseBiochemistry, 2011
- Structure of the Minimal Interface Between ApoE and LRPJournal of Molecular Biology, 2010
- Specificity of Binding of the Low Density Lipoprotein Receptor-related Protein to Different Conformational States of the Clade E Serpins Plasminogen Activator Inhibitor-1 and Proteinase Nexin-1Published by Elsevier BV ,2009
- Receptor-associated protein (RAP) has two high-affinity binding sites for the low-density lipoprotein receptor-related protein (LRP): consequences for the chaperone functions of RAPBiochemical Journal, 2009
- Unfolding of the RAP-D3 Helical Bundle Facilitates Dissociation of RAP−Receptor ComplexesBiochemistry, 2008
- Binding Site Structure of One LRP–RAP Complex:Implications for a Common Ligand–Receptor Binding MotifJournal of Molecular Biology, 2006
- Structure of an LDLR-RAP Complex Reveals a General Mode for Ligand Recognition by Lipoprotein ReceptorsMolecular Cell, 2006
- Identification of Coagulation Factor VIII A2 Domain Residues Forming the Binding Epitope for Low-Density Lipoprotein Receptor-Related Protein,Biochemistry, 2006
- Allosteric Modulation of Ligand Binding to Low Density Lipoprotein Receptor-related Protein by the Receptor-associated Protein Requires Critical Lysine Residues within Its Carboxyl-terminal DomainPublished by Elsevier BV ,2003