期刊
STRUCTURE
卷 23, 期 7, 页码 1271-1282出版社
CELL PRESS
DOI: 10.1016/j.str.2015.04.016
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资金
- Australian National Health and Medical Research Council (NHMRC) [1005896, 1058233]
- Hazel and Pip Appel Fund
- NHMRC Independent Research Institutes [361646]
- Victorian State Government
- Australian Postgraduate Award
- National Health and Medical Research Council of Australia [1058233] Funding Source: NHMRC
The homodimeric insulin and type 1 insulin-like growth factor receptors (IR and IGF-1R) share a common architecture and each can bind all three ligands within the family: insulin and insulin-like growth factors I and II (IGF-I and IFG-II). The receptor monomers also assemble as heterodimers, the primary ligand-binding sites of which each comprise the first leucine-rich repeat domain (L1) of one receptor type and an alpha-chain C-terminal segment (alpha CT) of the second receptor type. We present here crystal structures of IGF-I bound to such a hybrid primary binding site and of a ligand-free version of an IR aCT peptide bound to an IR L1 plus cysteine-rich domain construct (IR310.T). These structures, refined at 3.0-angstrom resolution, prove congruent to respective existing structures of insulin-complexed IR310.T and the intact apo-IR ectodomain. As such, they provide key missing links in the emerging, but sparse, repertoire of structures defining the receptor family.
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