1jl9

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{{STRUCTURE_1jl9| PDB=1jl9 | SCENE= }}
{{STRUCTURE_1jl9| PDB=1jl9 | SCENE= }}
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'''Crystal Structure of Human Epidermal Growth Factor'''
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===Crystal Structure of Human Epidermal Growth Factor===
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==Overview==
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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.
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The line below this paragraph, {{ABSTRACT_PUBMED_11438527}}, adds the Publication Abstract to the page
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(as it appears on PubMed at http://www.pubmed.gov), where 11438527 is the PubMed ID number.
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{{ABSTRACT_PUBMED_11438527}}
==About this Structure==
==About this Structure==
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[[Category: Dimerization]]
[[Category: Dimerization]]
[[Category: Growth factor]]
[[Category: Growth factor]]
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Revision as of 17:25, 1 July 2008

Image:1jl9.png

Template:STRUCTURE 1jl9

Crystal Structure of Human Epidermal Growth Factor

Template:ABSTRACT PUBMED 11438527

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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