PDBsum entry 4xst

Hormone/hormone receptor

PDB id: 4xst

Contents

Protein chains

287 a.a.

16 a.a.

Ligands

NAG-FUC

NAG ×3

SO4 ×2

PDB id:

4xst

Name:

Hormone/hormone receptor

Title:

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)

Structure:

Insulin receptor. Chain: e. Fragment: l1-cr, unp residues 28-377. Synonym: ir. Engineered: yes. Insulin receptor. Chain: f. Fragment: alpha-ct peptide, unp residues 697-719. Synonym: ir.

Source:

Homo sapiens. Human. Organism_taxid: 9606. Gene: insr. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell_line: lec 8 mutant cho cell. Synthetic: yes. Rattus norvegicus.

Resolution:

3.00Å R-factor: 0.219 R-free: 0.262

Authors:

J.G.Menting,C.F.Lawrence,G.K.-W.Kong,M.C.Lawrence

Key ref:

J.G.Menting et al. (2015). Structural Congruency of Ligand Binding to the Insulin and Insulin/Type 1 Insulin-like Growth Factor Hybrid Receptors. Structure, 23, 1271-1282. PubMed id: 26027733 DOI: 10.1016/j.str.2015.04.016

Date:

22-Jan-15 Release date: 10-Jun-15

Protein chain

P06213  (INSR_HUMAN) -  Insulin receptor from Homo sapiens

Seq: 1382 a.a.

Struc: 287 a.a.*

Protein chain

P15127  (INSR_RAT) -  Insulin receptor from Rattus norvegicus

Seq: 1383 a.a.

Struc: 16 a.a.

* PDB and UniProt seqs differ at 1 residue position (black cross)

Enzyme reactions

• Enzyme class: Chains E, F: E.C.2.7.10.1 - receptor protein-tyrosine kinase.
• Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H⁺

L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] (Bound ligand (Het Group name = NAG) matches with 41.38% similarity) + ADP + H(+)

Molecule diagrams generated from .mol files obtained from the KEGG ftp site

Added reference

DOI no: 10.1016/j.str.2015.04.016

Structure 23:1271-1282 (2015)

PubMed id: 26027733

Structural Congruency of Ligand Binding to the Insulin and Insulin/Type 1 Insulin-like Growth Factor Hybrid Receptors.

J.G.Menting, C.F.Lawrence, G.K.Kong, M.B.Margetts, C.W.Ward, M.C.Lawrence.

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.