The insulin receptor: from protein sequence to structure.
Sequences of the insulin receptor (IR), the type-I insulin-like growth-factor receptor (IGFR) and the insulin-receptor-related receptor show that they belong to a homologous family but, until recently, have given few clues about their structures. Three repeats of fibronectin type III have been identified close to the membrane. Although the N-terminal L1, Cys-rich and L2 domains of the IGFR have been identified from their sequences and their structures determined by X-ray crystallography, little is known of their relative positions in the complete receptor in vivo. Here, we ask what can be learnt further from the analysis of sequences, about the structure, organization and function of the extracellular regions of the IR family.
Department of Biochemistry, University of Cambridge, UK.
C
C
Marino-Buslje
M
M
Martin-Martinez
K
K
Mizuguchi
K
K
Siddle
T L
TL
Blundell
D000595:Amino Acid Sequence; D000818:Animals; D003545:Cysteine / Q000737:chemistry; D004220:Disulfides; D005353:Fibronectins / Q000737:chemistry; D006801:Humans; D008954:Models, Biological; D008969:Molecular Sequence Data; D017433:Protein Structure, Secondary; D017434:Protein Structure, Tertiary; D011972:Receptor, Insulin / Q000737:chemistry*; D017451:Receptors, Somatomedin / Q000737:chemistry*
D004220:Disulfides; D005353:Fibronectins; D017451:Receptors, Somatomedin; D011972:Receptor, Insulin; C066542:insulin receptor-related receptor; D003545:Cysteine