1jl9

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[[Image:1jl9.jpg|left|200px]]<br /><applet load="1jl9" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jl9.jpg|left|200px]]
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caption="1jl9, resolution 3.&Aring;" />
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'''Crystal Structure of Human Epidermal Growth Factor'''<br />
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{{Structure
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|PDB= 1jl9 |SIZE=350|CAPTION= <scene name='initialview01'>1jl9</scene>, resolution 3.&Aring;
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''Crystal Structure of Human Epidermal Growth Factor'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1JL9 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JL9 OCA].
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1JL9 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JL9 OCA].
==Reference==
==Reference==
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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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11438527 11438527]
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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:[http://www.ncbi.nlm.nih.gov/pubmed/11438527 11438527]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: growth factor]]
[[Category: growth factor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:23:55 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:04:59 2008''

Revision as of 10:05, 20 March 2008


PDB ID 1jl9

Drag the structure with the mouse to rotate
, resolution 3.Å
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Human Epidermal Growth Factor


Contents

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 disease associated with this structure: Hypomagnesemia 4, renal OMIM:[131530]

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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