1jl9

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spinqualitylabelsall models 1jl9, resolution 3.Å Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

Crystal Structure of Human Epidermal Growth Factor

Contents 1 Overview 2 Disease 3 About this Structure 4 Reference

Overview

Epidermal growth factor (EGF) is a typical growth-stimulating peptide and, functions by binding to specific cell-surface receptors and inducing, dimerization of the receptors. Little is known about the molecular, mechanism of EGF-induced dimerization of EGF receptors. The crystal, structure of human EGF has been determined at pH 8.1. There are two human, EGF molecules A and B in the asymmetric unit of the crystals, which form a, potential dimer. Importantly, a number of residues known to be, indispensable for EGF binding to its receptor are involved in the, interface between the two EGF molecules, suggesting a crucial role of EGF, dimerization in the EGF-induced dimerization of receptors. In addition, the crystal structure of EGF shares the main features of the NMR structure, of mouse EGF determined at pH 2.0, but structural comparisons between, different models have revealed new detailed features and properties of the, EGF structure.

Disease

Known diseases associated with this structure: Adenocarcinoma of lung, response to tyrosine kinase inhibitor in OMIM:[131550], Nonsmall cell lung cancer, response to tyrosine kinase inhibitor in OMIM:[131550], Nonsmall cell lung cancer, susceptibility to OMIM:[131550]

About this Structure

1JL9 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of human epidermal growth factor and its dimerization., Lu HS, Chai JJ, Li M, Huang BR, He CH, Bi RC, J Biol Chem. 2001 Sep 14;276(37):34913-7. Epub 2001 Jul 3. PMID:11438527

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