2CNJ
NMR studies on the interaction of Insulin-Growth Factor II (IGF-II) with IGF2R domain 11
Summary for 2CNJ
| Entry DOI | 10.2210/pdb2cnj/pdb |
| Related | 1E6F 1GP0 1GP3 1GQB 1JPL 1JWG 1LF8 |
| Descriptor | CATION-INDEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR (1 entity in total) |
| Functional Keywords | transport, polymorphism, glycoprotein, transmembrane, igf2r, cancer, membrane, receptor, lysosome, insulin-like growth factor-ii |
| Biological source | HOMO SAPIENS (HUMAN) |
| Total number of polymer chains | 1 |
| Total formula weight | 16651.85 |
| Authors | Williams, C.,Prince, S.,Zaccheo, O.,Hassan, A.B.,Crosby, J.,Crump, M. (deposition date: 2006-05-22, release date: 2007-05-22, Last modification date: 2024-05-15) |
| Primary citation | Williams, C.,Rezgui, D.,Prince, S.N.,Zaccheo, O.J.,Foulstone, E.J.,Forbes, B.E.,Norton, R.S.,Crosby, J.,Hassan, A.B.,Crump, M.P. Structural Insights Into the Interaction of Insulin-Like Growth Factor 2 with Igf2R Domain 11. Structure, 15:1065-, 2007 Cited by PubMed Abstract: The insulin-like growth factor II/mannose-6-phosphate receptor (IGF2R) mediates trafficking of mannose-6-phosphate (M6P)-containing proteins and the mitogenic hormone IGF2. IGF2R also plays an important role as a tumor suppressor, as mutation is frequently associated with human carcinogenesis. IGF2 binds to domain 11, one of 15 extracellular domains on IGF2R. The crystal structure of domain 11 and the solution structure of IGF2 have been reported, but, to date, there has been limited success when using crystallography to study the interaction of IGFs with their binding partners. As an approach to investigate the interaction between IGF2 and IGF2R, we have used heteronuclear NMR in combination with existing mutagenesis data to derive models of the domain 11-IGF2 complex by using the program HADDOCK. The models reveal that the molecular interaction is driven by critical hydrophobic residues on IGF2 and IGF2R, while a ring of flexible, charged residues on IGF2R may modulate binding. PubMed: 17850746DOI: 10.1016/J.STR.2007.07.007 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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