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1mox

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This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

1mox, resolution 2.50Å ()

Ligands:

, , ,

Non-Standard Residues:

, ,

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

Domains:

Recep_L_domain, FU, Furin-like

Related:

1igr, 1m6b, 2tgf

Structural annotation:
Resources:	CATH : 1Moxc00, 1Moxd00 InterPro : Ipr000719, Ipr000494, Ipr006211, Ipr006212, Ipr001245, Ipr009030, Ipr008266, Ipr011009, Ipr013032, Ipr006210, Ipr006209, Ipr001336, Ipr000742, Ipr015497 Pfam : PF01030, PF00757, PF00008 SCOP : d1moxa3, d1moxa1, d1moxa2, d1moxa4, d1moxb4, d1moxb1, d1moxb3, d1moxb2, d1moxc_, d1moxd_ UniProt : P00533, P01135

Functional annotation:
Resources:	GeneCard : TGFA
Cellular component:	plasma membrane AP-2 adaptor complex extracellular space membrane endosome cytoplasm nucleus integral to membrane soluble fraction integral to plasma membrane
Biological process:	positive regulation of phosphorylation cell cycle positive regulation of nitric oxide biosynthetic process cell proliferation protein amino acid phosphorylation transmembrane receptor protein tyrosine kinase signaling pathway positive regulation of cell proliferation cell-cell adhesion activation of phospholipase C activity regulation of peptidyl-tyrosine phosphorylation negative regulation of cell cycle signal transduction response to stress cell surface receptor linked signal transduction ossification protein insertion into membrane positive regulation of MAP kinase activity epidermal growth factor receptor signaling pathway regulation of nitric-oxide synthase activity positive regulation of epithelial cell proliferation positive regulation of cell migration calcium-dependent phospholipase A2 activation activation of MAPK activity positive regulation of mitosis positive regulation of epidermal growth factor receptor activity angiogenesis
Molecular function:	double-stranded DNA binding protein binding MAP/ERK kinase kinase activity protein kinase activity transmembrane receptor protein tyrosine kinase activity nitric-oxide synthase regulator activity protein-tyrosine kinase activity transferase activity ATP binding identical protein binding kinase activity epidermal growth factor receptor activity protein heterodimerization activity actin filament binding nucleotide binding transmembrane receptor activity receptor activity epidermal growth factor receptor activating ligand activity glycoprotein binding MAP kinase kinase activity growth factor activity signal transducer activity

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB

Coordinates:

save as pdb, mmCIF, xml

1 Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha
2 Disease
3 About this Structure
4 Reference

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

Publication Abstract from PubMed

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.

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

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Disease

Known disease 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 4 chains structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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. Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha. Cell. 2002 Sep 20;110(6):763-73. PMID:12297049

Page seeded by OCA on Tue Feb 17 03:43:18 2009

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Retrieved from "http://www.proteopedia.org/wiki/index.php/1mox"

1mox

From Proteopedia

Contents

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

Disease

About this Structure

Reference

Proteopedia Page Contributors and Editors (what is this?)

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