First time at Proteopedia? Click on the green links: they change the 3D image. Click and drag the molecules. Proteopedia is a 3D, interactive encyclopedia of proteins, RNA, DNA and other molecules. With a free user account, you can edit pages in Proteopedia. Visit the Main Page to learn more.

1ivo

From Proteopedia

Jump to: navigation, search

1ivo, resolution 3.30Å ()

Sites:

, , , , , , , , and

Ligands:

Activity:

Transferase, with EC number and 2.7.10.2 2.7.10.1 and 2.7.10.2

Related:

1jl9

Structural annotation:
Resources:	CATH : 1Ivoc00, 1Ivod00 InterPro : Ipr006211, Ipr000719, Ipr009030, Ipr006212, Ipr001245, Ipr008266, Ipr011009, Ipr000494, Ipr000742, Ipr001336, Ipr006209, Ipr000152, Ipr011042, Ipr001881, Ipr006210, Ipr013032, Ipr013091, Ipr000033 Pfam : PF00757, PF01030, PF00008 SCOP : d1ivoa3, d1ivoa4, d1ivoa1, d1ivoa2, d1ivob2, d1ivob3, d1ivob1, d1ivob4, d1ivoc_, d1ivod_ UniProt : P00533, P01133

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

Evolutionary conservation:

Toggle Conservation Colors:

Rows = identical sequences:

Further Information:

Caveats,

Explanation,
Complete Results at ConSurfDB

Resources:

FirstGlance, OCA, PDBsum, RCSB, TOPSAN

Coordinates:

save as pdb, mmCIF, xml

1 Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains.
2 About this Structure
3 See Also
4 Reference

Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains.

Publication Abstract from PubMed

Epidermal growth factor (EGF) regulates cell proliferation and differentiation by binding to the EGF receptor (EGFR) extracellular region, comprising domains I-IV, with the resultant dimerization of the receptor tyrosine kinase. In this study, the crystal structure of a 2:2 complex of human EGF and the EGFR extracellular region has been determined at 3.3 A resolution. EGFR domains I-III are arranged in a C shape, and EGF is docked between domains I and III. The 1:1 EGF*EGFR complex dimerizes through a direct receptor*receptor interaction, in which a protruding beta-hairpin arm of each domain II holds the body of the other. The unique "receptor-mediated dimerization" was verified by EGFR mutagenesis.

Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains., Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M, Yokoyama S, Cell. 2002 Sep 20;110(6):775-87. PMID:12297050

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

About this Structure

1ivo is a 4 chain structure of Epidermal Growth Factor Receptor with sequence from Homo sapiens. The June 2010 RCSB PDB Molecule of the Month feature on Epidermal Growth Factor Receptor by David Goodsell is 10.2210/rcsb_pdb/mom_2010_6. Full crystallographic information is available from OCA.

Reference

Ogiso H, Ishitani R, Nureki O, Fukai S, Yamanaka M, Kim JH, Saito K, Sakamoto A, Inoue M, Shirouzu M, Yokoyama S. Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell. 2002 Sep 20;110(6):775-87. PMID:12297050

Proteopedia Page Contributors and Editors (what is this?)

OCA

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

1ivo

From Proteopedia

Contents

Crystal Structure of the Complex of Human Epidermal Growth Factor and Receptor Extracellular Domains.

About this Structure

See Also

Reference

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

random

Search

Toolbox