1mox

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[[Image:1mox.gif|left|200px]]<br /><applet load="1mox" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1mox.gif|left|200px]]
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caption="1mox, resolution 2.5&Aring;" />
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'''Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha'''<br />
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{{Structure
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|PDB= 1mox |SIZE=350|CAPTION= <scene name='initialview01'>1mox</scene>, resolution 2.5&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=PT:PLATINUM+(II)+ION'>PT</scene>, <scene name='pdbligand=CD:CADMIUM+ION'>CD</scene> and <scene name='pdbligand=CL:CHLORIDE ION'>CL</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2]
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|GENE= EGFR ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]), TGFA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1MOX is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=PT:'>PT</scene>, <scene name='pdbligand=CD:'>CD</scene> and <scene name='pdbligand=CL:'>CL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Transferase Transferase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=2.7.10.1 and 2.7.10.2 2.7.10.1 and 2.7.10.2] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MOX OCA].
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1MOX is a [[Protein complex]] structure of sequences 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=1MOX OCA].
==Reference==
==Reference==
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Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha., Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Zhu HJ, Walker F, Frenkel MJ, Hoyne PA, Jorissen RN, Nice EC, Burgess AW, Ward CW, Cell. 2002 Sep 20;110(6):763-73. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12297049 12297049]
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Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha., Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Zhu HJ, Walker F, Frenkel MJ, Hoyne PA, Jorissen RN, Nice EC, Burgess AW, Ward CW, Cell. 2002 Sep 20;110(6):763-73. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12297049 12297049]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Protein complex]]
[[Category: Protein complex]]
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[[Category: receptor]]
[[Category: receptor]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:57:33 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:14 2008''

Revision as of 10:46, 20 March 2008

Image:1mox.gif


PDB ID 1mox

Drag the structure with the mouse to rotate
, resolution 2.5Å
Ligands: , , and
Gene: EGFR (Homo sapiens), TGFA (Homo sapiens)
Activity: Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2
Coordinates: save as pdb, mmCIF, xml



Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha


Contents

Overview

We report the crystal structure, at 2.5 A resolution, of a truncated human EGFR ectodomain bound to TGFalpha. TGFalpha interacts with both L1 and L2 domains of EGFR, making many main chain contacts with L1 and interacting with L2 via key conserved residues. The results indicate how EGFR family members can bind a family of highly variable ligands. In the 2:2 TGFalpha:sEGFR501 complex, each ligand interacts with only one receptor molecule. There are two types of dimers in the asymmetric unit: a head-to-head dimer involving contacts between the L1 and L2 domains and a back-to-back dimer dominated by interactions between the CR1 domains of each receptor. Based on sequence conservation, buried surface area, and mutagenesis experiments, the back-to-back dimer is favored to be biologically relevant.

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

1MOX is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha., Garrett TP, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Zhu HJ, Walker F, Frenkel MJ, Hoyne PA, Jorissen RN, Nice EC, Burgess AW, Ward CW, Cell. 2002 Sep 20;110(6):763-73. PMID:12297049

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