Abstract:
:The insulin receptor family consists of the homologous tyrosine kinase receptors, insulin receptor (IR), insulin-like growth factor 1 receptor (IGF1R) and insulin receptor-related receptor. The three-dimensional structures of the tyrosine kinase domain of the IR and the first three extracellular domains (L1, Cys-rich and L2) of the IGF1R are known. Here we present evidence that the connecting domain of the IR family is a member of the fibronectin type II (FnIII) superfamily. Structure-based alignment of FnIII domains reveals several key residues that are also conserved in the sequence of the connecting domain. The alignment of the connecting domain with FnIII domains is in good agreement with secondary structure prediction. A model of the connecting domain shows a hydrophobic core formed by the conserved residues and is consistent with previously known biochemical data. This suggests that the IR family contains three FnIII domains in tandem in the extracellular juxtamembrane region.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Marino-Buslje C,Mizuguchi K,Siddle K,Blundell TLdoi
10.1016/s0014-5793(98)01509-9subject
Has Abstractpub_date
1998-12-18 00:00:00pages
331-6issue
2eissn
0014-5793issn
1873-3468pii
S0014-5793(98)01509-9journal_volume
441pub_type
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