Carbohydrate recognition by the mannose-6-phosphate receptors. Curr Opin Struct Biol 2009 Oct;19(5):534-42
Date
10/06/2009Pubmed ID
19801188Pubmed Central ID
PMC2771201DOI
10.1016/j.sbi.2009.09.002Scopus ID
2-s2.0-70349882101 (requires institutional sign-in at Scopus site) 69 CitationsAbstract
The two P-type lectins, the 46kDa cation-dependent mannose-6-phosphate (Man-6-P) receptor (CD-MPR), and the 300kDa cation-independent Man-6-P receptor (CI-MPR), are the founding members of the growing family of mannose-6-phosphate receptor homology (MRH) proteins. A major cellular function of the MPRs is to transport Man-6-P-containing acid hydrolases from the Golgi to endosomal/lysosomal compartments. Recent advances in the structural analyses of both CD-MPR and CI-MPR have revealed the structural basis for phosphomannosyl recognition by these receptors and provided insights into how the receptors load and unload their cargo. A surprising finding is that the CD-MPR is dynamic, with at least two stable quaternary states, the open (ligand-bound) and closed (ligand-free) conformations, similar to those of hemoglobin. Ligand binding stabilizes the open conformation; changes in the pH of the environment at the cell surface and in endosomal compartments weaken the ligand-receptor interaction and/or weaken the electrostatic interactions at the subunit interface, resulting in the closed conformation.
Author List
Kim JJ, Olson LJ, Dahms NMAuthors
Nancy M. Dahms PhD Professor in the Biochemistry department at Medical College of WisconsinJung Ja P. Kim PhD Professor in the Biochemistry department at Medical College of Wisconsin
Linda J. Olson PhD Assistant Professor in the Biophysics department at Medical College of Wisconsin
MESH terms used to index this publication - Major topics in bold
AnimalsBinding Sites
Carbohydrate Metabolism
Carbohydrates
Humans
Ligands
Protein Conformation
Receptor, IGF Type 2
