Motion in Insulin Receptor Kinase [irk]

[ jump to morphs ]

Classification [D-h-2]

Structures 1IRK Apo form (unphosphorylated) [ PartsList ] 1IR3 Active, bound to nucleotide and peptide [ PartsList ]

Description Classic kinase domain closure upon nucleotide and substrate binding. Phosphorylation of the active loop also results in a large conformational change for this segment, which occludes the active site in the inactive structure.

References Hubbard SR; Wei L; Ellis L; Hendrickson WA (1994). Crystal structure of the tyrosine kinase domain of the human insulin receptor. Nature 372: 746-54. [Medline info for 95089813] S R Hubbard (1997). Crystal structure of the activated insulin receptor tyrosine kinase in complex with peptide substrate and ATP analog. EMBO J, 16:5572-81 [Medline info for 9312016] Y Ebina, L Ellis, K Jarnagin, M Edery, L Graf, E Clauser, J H Ou, F Masiarz, Y W Kan, I D Goldfine (1985). The human insulin receptor cDNA: the structural basis for hormone-activated transmembrane signalling. Cell, 40:747-58 [Medline info for 2859121]

GO terms associated with structures Molecular function transmembrane receptor protein tyrosine kinase activity, epidermal growth factor receptor activity, ATP binding, protein kinase activity, protein-tyrosine kinase activity Cellular component membrane Biological process transmembrane receptor protein tyrosine kinase signaling pathway, protein amino acid phosphorylation

Morphs

[ show all images ]

Best representative Morph Morph name Structure #1 Structure #2 Residues [ ] [ ]

---

Copyright 1995-2005 M. Gerstein, W. Krebs, S. Flores, N. Echols, and others
Email: Mark.Gerstein _at_ yale.edu