Structure of the human cation-independent mannose 6-phosphate/IGF2 receptor domains 7–11 uncovers the mannose 6-phosphate binding site of domain 9
The cation-independent mannose 6-phosphate (M6P)/Insulin-like growth factor-2 receptor (CI-MPR/IGF2R) is an ∼300 kDa transmembrane protein responsible for trafficking M6P-tagged lysosomal hydrolases and internalizing IGF2. The extracellular region of the CI-MPR has 15 homologous domains, including M...
Hlavní autoři: | Bochel, AJ, Williams, C, McCoy, AJ, Hoppe, H-J, Winter, AJ, Nicholls, RD, Harlos, K, Jones, EY, Berger, I, Hassan, AB, Crump, MP |
---|---|
Médium: | Journal article |
Jazyk: | English |
Vydáno: |
Cell Press
2020
|
Podobné jednotky
-
Interactions of IGF-II with the IGF2R/cation-independent mannose-6-phosphate receptor mechanism and biological outcomes.
Autor: Brown, J, a další
Vydáno: (2009) -
The host mannose-6-phosphate pathway and viral infection
Autor: Qincheng Liu, a další
Vydáno: (2024-01-01) -
In vitro binding of HFE to the cation-independent mannose-6 phosphate receptor.
Autor: Schimanski, L, a další
Vydáno: (2009) -
Kinetics of insulin-like growth factor II (IGF-II) interaction with domain 11 of the human IGF-II/mannose 6-phosphate receptor: function of CD and AB loop solvent-exposed residues.
Autor: Zaccheo, O, a další
Vydáno: (2006) -
Real time kinetics of insulin-like growth factor II (IGF-II) interaction with the IGF-II/mannose 6-phosphate receptor: the effects of domain 13 and pH.
Autor: Linnell, J, a další
Vydáno: (2001)