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(1)
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Electron Microscopy
(2)
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(63)
Campbell ID
(2)
Cooke RM
(2)
Harvey TS
(2)
Huang Y
(2)
Karandur D
(2)
Kuriyan J
(2)
Li YC
(2)
Merk A
(2)
Miller K
(2)
Montelione GT
(2)
Moy FJ
(2)
Ognjenovic J
(2)
Rauenbuehler P
(2)
Scheraga HA
(2)
Subramaniam S
(2)
Tappin MJ
(2)
Wilkinson AJ
(2)
Winkler ME
(2)
Adams TE
(1)
Atwell S
(1)
Bian Y
(1)
Boyles JS
(1)
Brennan L
(1)
Brown FK
(1)
Brown SC
(1)
Burgess AW
(1)
Chamberlin S
(1)
Chamberlin SG
(1)
Clawson DK
(1)
Davies D
(1)
Davies DE
(1)
Druzina Z
(1)
Elleman TC
(1)
Frenkel MJ
(1)
Garrett TP
(1)
Garrett TPJ
(1)
Guo Q
(1)
Heuer JG
(1)
Hoyne PA
(1)
Jeffs PW
(1)
Jorissen RN
(1)
Josef GH
(1)
Kline TP
(1)
Kopple KD
(1)
Lou M
(1)
Lovrecz GO
(1)
Manolopoulou M
(1)
McKern NM
(1)
Mueller L
(1)
Nice EC
(1)
Puddicombe S
(1)
Puddicombe SM
(1)
Schilling AB
(1)
Tang W-J
(1)
Tang WJ
(1)
Turner D
(1)
Turner DL
(1)
Walker F
(1)
Ward CW
(1)
Weichert K
(1)
Witcher DR
(1)
Zhu H-J
(1)
Zhu HJ
(1)
Homo / hetero assembly
(2)
homo
(6)
hetero
(5)
Assembly composition
(2)
protein structure
(6)
protein/protein complex
(5)
Assembly polymer count
(4)
monomer
(6)
tetramer
(3)
dimer
(1)
trimer
(1)
Resolution distribution
2.0 - 2.5
(2)
2.5 - 3
(1)
3.0 - 3.5
(1)
3.5 - 4
(1)
Release year distribution
1990 - 1995
(3)
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(2)
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Eur J Biochem
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Cell
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Macromolecules
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Eukaryota
(11)
Organism name
(2)
Homo sapiens
(11)
Mus musculus
(1)
Molecule name
(17)
EGF-like TGF
(11)
ETGF
(11)
Protransforming growth factor alpha
(11)
TGF type 1
(11)
TGF-alpha
(11)
Transforming growth factor alpha
(11)
Epidermal growth factor receptor
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Proto-oncogene c-ErbB-1
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Receptor tyrosine-protein kinase erbB-1
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Abeta-degrading protease
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EGF
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(11)
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(7)
TGFA
(11)
EGFR
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ERBB
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ERBB1
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HER1
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Egf
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IDE
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Transforming growth factor alpha
(4)
Epidermal growth factor receptor
(3)
Epiregulin Antibody LY3016859 Fab Heavy Chain
(1)
Epiregulin Antibody LY3016859 Fab Light Chain
(1)
Insulin-degrading enzyme
(1)
Interacting ligands
(8)
ZN : ZINC ION
(2)
BMA : beta-D-mannopyranose
(1)
CD : CADMIUM ION
(1)
CL : CHLORIDE ION
(1)
FUC : alpha-L-fucopyranose
(1)
MAN : alpha-D-mannopyranose
(1)
NAG : 2-acetamido-2-deoxy-beta-D-glucopyranose
(1)
PT : PLATINUM (II) ION
(1)
Function and Biology
EC number / name
(2)
2.7.10.1 : Receptor protein-tyrosine kinase
(3)
3.4.24.56 : Insulysin
(1)
Biological function
(23)
ATP binding
(3)
protein kinase activity
(2)
protein tyrosine kinase activity
(2)
ATP hydrolysis activity
(1)
amyloid-beta binding
(1)
beta-endorphin binding
(1)
catalytic activity
(1)
endopeptidase activity
(1)
hydrolase activity
(1)
identical protein binding
(1)
insulin binding
(1)
metal ion binding
(1)
metalloendopeptidase activity
(1)
metallopeptidase activity
(1)
nucleotide binding
(1)
peptidase activity
(1)
peptide binding
(1)
peptide hormone binding
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protein binding
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protein homodimerization activity
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protein-containing complex binding
(1)
virus receptor activity
(1)
zinc ion binding
(1)
Biological process
(21)
cell surface receptor protein tyrosine kinase signaling pathway
(2)
protein phosphorylation
(2)
amyloid-beta clearance
(1)
amyloid-beta clearance by cellular catabolic process
(1)
amyloid-beta metabolic process
(1)
antigen processing and presentation of endogenous peptide antigen via MHC class I
(1)
bradykinin catabolic process
(1)
hormone catabolic process
(1)
insulin catabolic process
(1)
insulin metabolic process
(1)
insulin receptor signaling pathway
(1)
negative regulation of proteolysis
(1)
peptide catabolic process
(1)
positive regulation of protein binding
(1)
positive regulation of protein catabolic process
(1)
protein catabolic process
(1)
proteolysis
(1)
proteolysis involved in protein catabolic process
(1)
regulation of aerobic respiration
(1)
symbiont entry into host cell
(1)
ubiquitin recycling
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Biological cell component
(15)
membrane
(3)
basolateral plasma membrane
(1)
cell surface
(1)
cytoplasm
(1)
cytosol
(1)
cytosolic proteasome complex
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external side of plasma membrane
(1)
extracellular exosome
(1)
extracellular region
(1)
extracellular space
(1)
mitochondrion
(1)
nucleus
(1)
peroxisomal matrix
(1)
peroxisome
(1)
plasma membrane
(1)
Sequence and Structure classification
SCOP fold
(2)
Knottins (small inhibitors, toxins, lectins)
(7)
Leucine-rich repeat, LRR (right-handed beta-alpha superhelix)
(1)
SCOP family
(3)
EGF-type module
(7)
Growth factor receptor domain
(1)
L domain
(1)
CATH class
(2)
Mainly Beta
(8)
Alpha Beta
(2)
CATH topology
(4)
Laminin
(8)
24 nucleotide stem-loop, u2 snrnp hairpin iv. U2 a'; Chain A
(1)
Cytochrome Bc1 Complex; Chain A, domain 1
(1)
Hormone Receptor, Insulin-like Growth Factor Receptor 1; Chain A domain 2
(1)
Pfam accession / name
(9)
PF00757 : Furin-like
(3)
PF01030 : Recep_L_domain
(3)
PF07714 : PK_Tyr_Ser-Thr
(2)
PF14843 : GF_recep_IV
(2)
PF21314 : TM_ErbB1
(2)
PF00008 : EGF
(1)
PF00675 : Peptidase_M16
(1)
PF05193 : Peptidase_M16_C
(1)
PF16187 : Peptidase_M16_M
(1)
Experimental Information
Diffraction protocol
(1)
Single wavelength
(3)
Diffraction radiation source type
(2)
Synchrotron
(2)
Rotating anode
(1)
Diffraction source
(3)
APS BEAMLINE 19-ID
(1)
APS BEAMLINE 31-ID
(1)
RIGAKU RU300
(1)
Synchrotron site
(1)
APS
(2)
Diffraction detector type
(2)
Image plate
(2)
CCD
(1)
Refinement software
(2)
REFMAC
(2)
CNS
(1)
EM microscope model
(1)
FEI TITAN KRIOS
(2)
EM detector name
(1)
GATAN K3 (6k x 4k)
(2)
NMR
NMR software packages
(5)
DISMAN
(1)
DSPACE
(1)
ECEPP/3
(1)
INDYANA
(1)
X-PLOR
(1)
NMR Field Strength
400.0 - 500
(1)
500.0 - 600
(1)
Representative Structures
Representative Structures
Entries
Macromolecules
Compounds
Protein families
Entries 1 to 10 of 11
Select all entries on this page
Crystal Structure of Human Epidermal Growth Factor Receptor (residues 1-501) in complex with TGF-alpha
Garrett TPJ, McKern NM, Lou M, Elleman TC, Adams TE, Lovrecz GO, Zhu H-J, Walker F, Frenkel MJ, Hoyne PA, Jorissen RN, Nice EC, Burgess AW, Ward CW
Cell
(2002)
[PMID: 12297049 ]
Source organism: Homo sapiens
Assembly composition: protein/protein complex
Carbohydrate polymer components:
Molecule 1 -
FUC(1), NAG(2)
Molecule 2 -
BMA(1), MAN(1), NAG(2)
Molecule 3 -
BMA(1), FUC(1), NAG(2)
Molecule 4 -
NAG(2)
Assembly name:
Epidermal growth factor receptor and Transforming growth factor alpha
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-132704 (Preferred)
search this ID
THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA
Harvey TS, Wilkinson AJ, Tappin MJ, Cooke RM, Campbell ID
Eur J Biochem
(1991)
[PMID: 2050136 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Transforming growth factor alpha
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-134053 (Preferred)
search this ID

THE SOLUTION STRUCTURE OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA
Harvey TS, Wilkinson AJ, Tappin MJ, Cooke RM, Campbell ID
Eur J Biochem
(1991)
[PMID: 2050136 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Transforming growth factor alpha
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-134053 (Preferred)
search this ID

SOLUTION STRUCTURES OF HUMAN TRANSFORMING GROWTH FACTOR ALPHA DERIVED FROM 1*H NMR DATA
Kline TP, Brown FK, Brown SC, Jeffs PW, Kopple KD, Mueller L
Biochemistry
(1990)
[PMID: 2261437 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Transforming growth factor alpha
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-134053 (Preferred)
search this ID

TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 16 MODELS WITHOUT ENERGY MINIMIZATION
Moy FJ, Montelione GT, Scheraga HA
Biochemistry
(1993)
[PMID: 8338831 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Transforming growth factor alpha
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-134053 (Preferred)
search this ID

TYPE ALPHA TRANSFORMING GROWTH FACTOR, NMR, 15 MODELS AFTER ECEPP/3 ENERGY MINIMIZATION
Moy FJ, Montelione GT, Scheraga HA
Biochemistry
(1993)
[PMID: 8338831 ]
Source organism: Homo sapiens
Assembly composition: protein only structure
Assembly name:
Transforming growth factor alpha
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-134053 (Preferred)
search this ID

Cryo-EM structure of the extracellular module of the full-length EGFR bound to TGF-alpha. "tips-juxtaposed" conformation
Huang Y, Ognjenovic J, Karandur D, Miller K, Merk A, Subramaniam S, Kuriyan J
Elife
(2021)
[PMID: 34846302 ]
Source organism: Homo sapiens
Assembly composition: protein/protein complex
Assembly name:
Epidermal growth factor receptor and Transforming growth factor alpha
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-132704 (Preferred)
search this ID
Cryo-EM structure of the extracellular module of the full-length EGFR bound to TGF-alpha "tips-separated" conformation
Huang Y, Ognjenovic J, Karandur D, Miller K, Merk A, Subramaniam S, Kuriyan J
Elife
(2021)
[PMID: 34846302 ]
Source organism: Homo sapiens
Assembly composition: protein/protein complex
Assembly name:
Epidermal growth factor receptor and Transforming growth factor alpha
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-132704 (Preferred)
search this ID
Crystal structure of human insulin degrading enzyme in complex with transforming growth factor-alpha
Guo Q, Manolopoulou M, Tang W-J
J Mol Biol
(2010)
[PMID: 19896952 ]
Source organism: Homo sapiens
Assembly composition: protein/protein complex
Assembly name:
Insulin-degrading enzyme and Transforming growth factor alpha
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-134054 (Preferred)
search this ID
Solution Structure the mEGF/TGFalpha44-50 chimeric growth factor
Chamberlin SG, Brennan L, Puddicombe SM, Davies DE, Turner DL
Eur J Biochem
(2001)
[PMID: 11733021 ]
Source organisms: Mus musculus , Homo sapiens
Assembly composition: protein only structure
Assembly name:
Epidermal growth factor, Transforming growth factor alpha
(Preferred)
search this complex
PDBe complex ID:
PDB-CPX-134049 (Preferred)
search this ID
Entries 1 to 10 of 11