2CNJ

NMR studies on the interaction of Insulin-Growth Factor II (IGF-II) with IGF2R domain 11

2CNJ の概要

• エントリーDOI: 10.2210/pdb2cnj/pdb
• 関連するPDBエントリー: 1E6F 1GP0 1GP3 1GQB 1JPL 1JWG 1LF8
• 分子名称: CATION-INDEPENDENT MANNOSE-6-PHOSPHATE RECEPTOR (1 entity in total)
• 機能のキーワード: transport, polymorphism, glycoprotein, transmembrane, igf2r, cancer, membrane, receptor, lysosome, insulin-like growth factor-ii
• 由来する生物種: HOMO SAPIENS (HUMAN)
• タンパク質・核酸の鎖数: 1
• 化学式量合計: 16651.85

構造登録者

Williams, C.,Prince, S.,Zaccheo, O.,Hassan, A.B.,Crosby, J.,Crump, M. (登録日: 2006-05-22, 公開日: 2007-05-22, 最終更新日: 2024-05-15)

主引用文献

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

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: 17850746
DOI: 10.1016/J.STR.2007.07.007

実験手法

SOLUTION NMR