4XSS

Insulin-like growth factor I in complex with site 1 of a hybrid insulin receptor / Type 1 insulin-like growth factor receptor

Summary for 4XSS

• Entry DOI: 10.2210/pdb4xss/pdb
• Related: 3W11 3W12 3W13 3W14 4OGA 4XST
• Descriptor: Insulin-like growth factor I, Insulin receptor, Insulin-like growth factor receptor alpha-CT peptide, ... (7 entities in total)
• Functional Keywords: cell surface receptor/immune system, insulin receptor, ct peptide, insulin-like growth factor receptor, hormone receptor-hormone-immune system complex, hormone-hormone receptor complex, hormone/hormone receptor
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 3
• Total formula weight: 48126.83

Authors

Lawrence, C.,Kong, G.K.-W.,Menting, J.G.,Lawrence, M.C. (deposition date: 2015-01-22, release date: 2015-06-10, Last modification date: 2024-11-06)

Primary citation

Menting, J.G.,Lawrence, C.F.,Kong, G.K.,Margetts, M.B.,Ward, C.W.,Lawrence, M.C.
Structural Congruency of Ligand Binding to the Insulin and Insulin/Type 1 Insulin-like Growth Factor Hybrid Receptors.
Structure, 23:1271-1282, 2015

PubMed Abstract: 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 α-chain C-terminal segment (αCT) 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 αCT peptide bound to an IR L1 plus cysteine-rich domain construct (IR310.T). These structures, refined at 3.0-Å 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.

PubMed: 26027733
DOI: 10.1016/j.str.2015.04.016

Experimental method

X-RAY DIFFRACTION (3 Å)