4XST

Structure of the endoglycosidase-H treated L1-CR domains of the human insulin receptor in complex with residues 697-719 of the human insulin receptor (A-isoform)

Summary for 4XST

• Entry DOI: 10.2210/pdb4xst/pdb
• Descriptor: Insulin receptor, alpha-L-fucopyranose-(1-6)-2-acetamido-2-deoxy-beta-D-glucopyranose, 2-acetamido-2-deoxy-beta-D-glucopyranose, ... (5 entities in total)
• Functional Keywords: insulin receptor, insulin micro-receptor, hormone-hormone receptor complex, hormone/hormone receptor
• Biological source: Homo sapiens (Human); More
• Total number of polymer chains: 2
• Total formula weight: 40246.99

Authors

Menting, J.G.,Lawrence, C.F.,Kong, G.K.-W.,Lawrence, M.C. (deposition date: 2015-01-22, release date: 2015-06-10, Last modification date: 2024-11-20)

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)