PDBsum entry 1ivo

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protein ligands Protein-protein interface(s) links
Transferase/signaling protein PDB id
Protein chains
511 a.a. *
47 a.a. *
NAG ×8
Waters ×79
* Residue conservation analysis
PDB id:
Name: Transferase/signaling protein
Title: Crystal structure of the complex of human epidermal growth f receptor extracellular domains.
Structure: Epidermal growth factor receptor. Chain: a, b. Fragment: extracellular domains i, ii, ii and iv. Engineered: yes. Epidermal growth factor. Chain: c, d. Fragment: residues 1-53. Synonym: egf. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expressed in: escherichia coli. Expression_system_taxid: 562
Biol. unit: Dimer (from PQS)
3.30Å     R-factor:   0.255     R-free:   0.326
Authors: H.Ogiso,R.Ishitani,O.Nureki,S.Fukai,M.Yamanaka,J.H.Kim,K.Sai M.Shirouzu,S.Yokoyama,Riken Structural Genomics/proteomics Initiative (Rsgi)
Key ref:
H.Ogiso et al. (2002). Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains. Cell, 110, 775-787. PubMed id: 12297050 DOI: 10.1016/S0092-8674(02)00963-7
28-Mar-02     Release date:   16-Oct-02    
Go to PROCHECK summary

Protein chains
Pfam   ArchSchema ?
P00533  (EGFR_HUMAN) -  Epidermal growth factor receptor
1210 a.a.
511 a.a.
Protein chains
Pfam   ArchSchema ?
P01133  (EGF_HUMAN) -  Pro-epidermal growth factor
1207 a.a.
47 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure  CATH domain

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.  - Receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: ATP + a [protein]-L-tyrosine = ADP + a [protein]-L-tyrosine phosphate
Bound ligand (Het Group name = NAG)
matches with 47.62% similarity
+ [protein]-L-tyrosine phosphate
Molecule diagrams generated from .mol files obtained from the KEGG ftp site
 Gene Ontology (GO) functional annotation 
  GO annot!
  Cellular component     membrane   1 term 
  Biological process     transmembrane receptor protein tyrosine kinase signaling pathway   2 terms 
  Biochemical function     ATP binding     2 terms  


DOI no: 10.1016/S0092-8674(02)00963-7 Cell 110:775-787 (2002)
PubMed id: 12297050  
Crystal structure of the complex of human epidermal growth factor and receptor extracellular domains.
H.Ogiso, R.Ishitani, O.Nureki, S.Fukai, M.Yamanaka, J.H.Kim, K.Saito, A.Sakamoto, M.Inoue, M.Shirouzu, S.Yokoyama.
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.
  Selected figure(s)  
Figure 3.
Figure 3. Interactions between EGF and EGFREGF and the EGFR domains are colored in the same manner as in Figure 1, except for (B).(A) Mapping the interaction sites onto ribbon representations of EGFR and EGF. Three binding sites in the interface are outlined.(B) EGF structure. The A, B, and C loops are colored blue, green, and red, respectively. The other regions are pale green.(C) Stereo view of the interface at site 1. Only the side chains of interacting residues are shown. Dotted lines represent hydrogen bonds.(D) Stereo view of the interface at site 2.(E) Stereo view of the interface at site 3.
Figure 4.
Figure 4. Interactions between Each Receptor in the Dimer Interface(A) The binding region in the interface is outlined. Only the side chains of interacting residues are shown. EGF and the EGFR domains are colored in the same manner as in Figure 1.(B) Stereo view of an annealed omit map. Residues 240–260 and the residues within 3.5 Å from them of one EGRF molecule (orange) were omitted.(C) Stereo view of the interface from the view shown by the arrow in (A); the view is directed from the front side of domain I toward Y251 of the other receptor. Dotted lines represent hydrogen bonds.(D) Stereo view of the interface from the view shown by the arrow in (A); the view is directed from the back side of domain I toward Y251 of the other receptor.
  The above figures are reprinted by permission from Cell Press: Cell (2002, 110, 775-787) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

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PDB codes: 3ltf 3ltg
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PDB code: 3i2t
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PDB codes: 3g8k 3g8l
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PDB codes: 3bbt 3bbw 3bce
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PDB codes: 3c9a 3ca7 3cgu
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PDB codes: 3c08 3c09
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PDB codes: 3b2u 3b2v
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Expression and differential signaling of heregulins in pancreatic cancer cells.
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Epidermal growth factor receptor (EGFR) is transcriptionally induced by the Y-box binding protein-1 (YB-1) and can be inhibited with Iressa in basal-like breast cancer, providing a potential target for therapy.
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The insulin and EGF receptor structures: new insights into ligand-induced receptor activation.
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A monkey wrench in the kinase machine.
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The EGF receptor family: spearheading a merger of signaling and therapeutics.
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ErbB receptors: from oncogenes to targeted cancer therapies.
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Evolvable signaling networks of receptor tyrosine kinases: relevance of robustness to malignancy and to cancer therapy.
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17306385 M.Katz, I.Amit, and Y.Yarden (2007).
Regulation of MAPKs by growth factors and receptor tyrosine kinases.
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17468161 P.Liu, T.Sudhaharan, R.M.Koh, L.C.Hwang, S.Ahmed, I.N.Maruyama, and T.Wohland (2007).
Investigation of the dimerization of proteins from the epidermal growth factor receptor family by single wavelength fluorescence cross-correlation spectroscopy.
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17274834 R.Landgraf (2007).
HER2 therapy. HER2 (ERBB2): functional diversity from structurally conserved building blocks.
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17894821 S.F.Cummins, F.Xie, Vries, S.P.Annangudi, M.Misra, B.M.Degnan, J.V.Sweedler, G.T.Nagle, and C.H.Schein (2007).
Aplysia temptin - the 'glue' in the water-borne attractin pheromone complex.
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17339314 S.J.Chan, S.Nakagawa, and D.F.Steiner (2007).
Complementation analysis demonstrates that insulin cross-links both alpha subunits in a truncated insulin receptor dimer.
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17306972 S.R.Hubbard, and W.T.Miller (2007).
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Oligomerization of the EGF receptor investigated by live cell fluorescence intensity distribution analysis.
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17804794 W.D.Tolbert, J.Daugherty, C.Gao, Q.Xie, C.Miranti, E.Gherardi, G.V.Woude, and H.E.Xu (2007).
A mechanistic basis for converting a receptor tyrosine kinase agonist to an antagonist.
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PDB codes: 2qj2 2qj4
16829981 A.Citri, and Y.Yarden (2006).
EGF-ERBB signalling: towards the systems level.
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16531225 A.Sivasubramanian, G.Chao, H.M.Pressler, K.D.Wittrup, and J.J.Gray (2006).
Structural model of the mAb 806-EGFR complex using computational docking followed by computational and experimental mutagenesis.
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PDB codes: 2exp 2exq
16825199 C.M.Warren, K.Kani, and R.Landgraf (2006).
The N-terminal domains of neuregulin 1 confer signal attenuation.
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16865534 C.Sweeney, J.K.Miller, D.L.Shattuck, and K.L.Carraway (2006).
ErbB receptor negative regulatory mechanisms: implications in cancer.
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16963452 C.Zahnd, F.Pecorari, N.Straumann, E.Wyler, and A.Plückthun (2006).
Selection and characterization of Her2 binding-designed ankyrin repeat proteins.
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16537482 E.Gherardi, S.Sandin, M.V.Petoukhov, J.Finch, M.E.Youles, L.G.Ofverstedt, R.N.Miguel, T.L.Blundell, G.F.Vande Woude, U.Skoglund, and D.I.Svergun (2006).
Structural basis of hepatocyte growth factor/scatter factor and MET signalling.
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PDB codes: 2ced 2cee 2ceg 2cew
16533841 H.Shankaran, H.S.Wiley, and H.Resat (2006).
Modeling the effects of HER/ErbB1-3 coexpression on receptor dimerization and biological response.
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16433931 H.T.Chang, T.W.Pai, T.C.Fan, B.H.Su, P.C.Wu, C.Y.Tang, C.T.Chang, S.H.Liu, and M.D.Chang (2006).
A reinforced merging methodology for mapping unique peptide motifs in members of protein families.
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16499962 J.Ichinose, M.Morimatsu, T.Yanagida, and Y.Sako (2006).
Covalent immobilization of epidermal growth factor molecules for single-molecule imaging analysis of intracellular signaling.
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16546374 J.J.Gray (2006).
High-resolution protein-protein docking.
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16842869 J.Macdonald, Z.Li, W.Su, and L.J.Pike (2006).
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16267617 J.N.Contessa, A.Abell, R.B.Mikkelsen, K.Valerie, and R.K.Schmidt-Ullrich (2006).
Compensatory ErbB3/c-Src signaling enhances carcinoma cell survival to ionizing radiation.
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16411922 M.Date, H.Itaya, H.Matsui, and Y.Kikuchi (2006).
Secretion of human epidermal growth factor by Corynebacterium glutamicum.
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18360654 N.Starling, J.Neoptolemos, and D.Cunningham (2006).
Role of erlotinib in the management of pancreatic cancer.
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16597832 N.Y.Lee, T.L.Hazlett, and J.G.Koland (2006).
Structure and dynamics of the epidermal growth factor receptor C-terminal phosphorylation domain.
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16928683 P.P.Knowles, J.Murray-Rust, S.Kjaer, R.P.Scott, S.Hanrahan, M.Santoro, C.F.Ibáñez, and N.Q.McDonald (2006).
Structure and chemical inhibition of the RET tyrosine kinase domain.
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PDB codes: 2ivs 2ivt 2ivu 2ivv
17026767 R.A.Stein, and J.V.Staros (2006).
Insights into the evolution of the ErbB receptor family and their ligands from sequence analysis.
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16380971 S.Aifa, N.Miled, F.Frikha, M.R.Aniba, S.P.Svensson, and A.Rebai (2006).
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16788977 S.Kamath, and J.K.Buolamwini (2006).
Targeting EGFR and HER-2 receptor tyrosine kinases for cancer drug discovery and development.
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18377216 S.Meierjohann, T.Mueller, M.Schartl, and M.Buehner (2006).
A structural model of the extracellular domain of the oncogenic EGFR variant Xmrk.
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17032651 S.P.van der Woning, W.van Rotterdam, S.B.Nabuurs, H.Venselaar, S.Jacobs-Oomen, M.Wingens, G.Vriend, C.Stortelers, and E.J.van Zoelen (2006).
Negative constraints underlie the ErbB specificity of epidermal growth factor-like ligands.
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16889899 S.Sebastian, J.Settleman, S.J.Reshkin, A.Azzariti, A.Bellizzi, and A.Paradiso (2006).
The complexity of targeting EGFR signalling in cancer: from expression to turnover.
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16624867 V.P.Ramsauer, V.Pino, A.Farooq, C.A.Carothers Carraway, P.J.Salas, and K.L.Carraway (2006).
Muc4-ErbB2 complex formation and signaling in polarized CACO-2 epithelial cells indicate that Muc4 acts as an unorthodox ligand for ErbB2.
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16732286 W.A.Barton, D.Tzvetkova-Robev, E.P.Miranda, M.V.Kolev, K.R.Rajashankar, J.P.Himanen, and D.B.Nikolov (2006).
Crystal structures of the Tie2 receptor ectodomain and the angiopoietin-2-Tie2 complex.
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PDB codes: 2gy5 2gy7
16777603 X.Zhang, J.Gureasko, K.Shen, P.A.Cole, and J.Kuriyan (2006).
An allosteric mechanism for activation of the kinase domain of epidermal growth factor receptor.
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PDB codes: 2gs2 2gs6 2gs7
16355407 Y.S.Kim, R.Bhandari, J.R.Cochran, J.Kuriyan, and K.D.Wittrup (2006).
Directed evolution of the epidermal growth factor receptor extracellular domain for expression in yeast.
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16946702 Y.Teramura, J.Ichinose, H.Takagi, K.Nishida, T.Yanagida, and Y.Sako (2006).
Single-molecule analysis of epidermal growth factor binding on the surface of living cells.
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Ligand-induced dimer-tetramer transition during the activation of the cell surface epidermal growth factor receptor-A multidimensional microscopy analysis.
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15795223 A.N.Weber, M.C.Moncrieffe, M.Gangloff, J.L.Imler, and N.J.Gay (2005).
Ligand-receptor and receptor-receptor interactions act in concert to activate signaling in the Drosophila toll pathway.
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15880563 A.P.Venook (2005).
Epidermal growth factor receptor-targeted treatment for advanced colorectal carcinoma.
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The role of cetuximab in the treatment of squamous cell cancer of the head and neck.
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15611079 B.S.Kochupurakkal, D.Harari, A.Di-Segni, G.Maik-Rachline, L.Lyass, G.Gur, G.Kerber, A.Citri, S.Lavi, R.Eilam, V.Chalifa-Caspi, Z.Eshhar, E.Pikarsky, R.Pinkas-Kramarski, S.S.Bacus, and Y.Yarden (2005).
Epigen, the last ligand of ErbB receptors, reveals intricate relationships between affinity and mitogenicity.
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The inhibitory effect of ErbB2 on epidermal growth factor-induced formation of clathrin-coated pits correlates with retention of epidermal growth factor receptor-ErbB2 oligomeric complexes at the plasma membrane.
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15822127 C.Luo, L.Xu, S.Zheng, X.Luo, J.Shen, H.Jiang, X.Liu, and M.Zhou (2005).
Computational analysis of molecular basis of 1:1 interactions of NRG-1beta wild-type and variants with ErbB3 and ErbB4.
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15688065 C.P.Blobel (2005).
ADAMs: key components in EGFR signalling and development.
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16103229 D.S.Lidke, K.A.Lidke, B.Rieger, T.M.Jovin, and D.J.Arndt-Jovin (2005).
Reaching out for signals: filopodia sense EGF and respond by directed retrograde transport of activated receptors.
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16265350 G.N.Berta, B.Mognetti, M.Spadaro, E.Trione, A.Amici, G.Forni, F.Di Carlo, and F.Cavallo (2005).
Anti-HER-2 DNA vaccine protects Syrian hamsters against squamous cell carcinomas.
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16212492 G.Vert, J.L.Nemhauser, N.Geldner, F.Hong, and J.Chory (2005).
Molecular mechanisms of steroid hormone signaling in plants.
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16185155 J.G.Shelton, L.S.Steelman, S.L.Abrams, F.E.Bertrand, R.A.Franklin, M.McMahon, and J.A.McCubrey (2005).
The epidermal growth factor receptor gene family as a target for therapeutic intervention in numerous cancers: what's genetics got to do with it?
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15840573 K.Choowongkomon, C.R.Carlin, and F.D.Sönnichsen (2005).
A structural model for the membrane-bound form of the juxtamembrane domain of the epidermal growth factor receptor.
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PDB code: 1z9i
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Oligomers of ERBB3 have two distinct interfaces that differ in their sensitivity to disruption by heregulin.
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15480783 M.J.Oliveira, T.Lauwaet, G.De Bruyne, M.Mareel, and A.Leroy (2005).
Listeria monocytogenes produces a pro-invasive factor that signals via ErbB2/ErbB3 heterodimers.
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15864276 N.E.Hynes, and H.A.Lane (2005).
ERBB receptors and cancer: the complexity of targeted inhibitors.
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15660449 P.Aller, L.Voiry, N.Garnier, and M.Genest (2005).
Molecular dynamics (MD) investigations of preformed structures of the transmembrane domain of the oncogenic Neu receptor dimer in a DMPC bilayer.
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15596490 P.Bagossi, G.Horváth, G.Vereb, J.Szöllösi, and J.Tözsér (2005).
Molecular modeling of nearly full-length ErbB2 receptor.
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15920761 P.Hu, J.Feng, T.Zhou, J.Wang, B.Jing, M.Yu, M.Hu, X.Zhang, B.Shen, and N.Guo (2005).
In vivo identification of the interaction site of ErbB2 extracellular domain with its autoinhibitor.
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16203964 S.Bouyain, P.A.Longo, S.Li, K.M.Ferguson, and D.J.Leahy (2005).
The extracellular region of ErbB4 adopts a tethered conformation in the absence of ligand.
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PDB code: 2ahx
15837620 S.Li, K.R.Schmitz, P.D.Jeffrey, J.J.Wiltzius, P.Kussie, and K.M.Ferguson (2005).
Structural basis for inhibition of the epidermal growth factor receptor by cetuximab.
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PDB codes: 1yy8 1yy9
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An electrostatic engine model for autoinhibition and activation of the epidermal growth factor receptor (EGFR/ErbB) family.
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Phe45 of NRG2beta is critical for the affinity of NRG2beta for ErbB4 and for potent stimulation of ErbB4 signaling by NRG2beta*.
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15749770 T.Uyemura, H.Takagi, T.Yanagida, and Y.Sako (2005).
Single-molecule analysis of epidermal growth factor signaling that leads to ultrasensitive calcium response.
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16211506 X.Zuo, S.Li, J.Hall, M.R.Mattern, H.Tran, J.Shoo, R.Tan, S.R.Weiss, and T.R.Butt (2005).
Enhanced expression and purification of membrane proteins by SUMO fusion in Escherichia coli.
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15094157 A.Bennasroune, A.Gardin, D.Aunis, G.Crémel, and P.Hubert (2004).
Tyrosine kinase receptors as attractive targets of cancer therapy.
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15122207 A.Gschwind, O.M.Fischer, and A.Ullrich (2004).
The discovery of receptor tyrosine kinases: targets for cancer therapy.
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15166146 D.Alvarado, A.H.Rice, and J.B.Duffy (2004).
Bipartite inhibition of Drosophila epidermal growth factor receptor by the extracellular and transmembrane domains of Kekkon1.
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14732693 D.Mattoon, P.Klein, M.A.Lemmon, I.Lax, and J.Schlessinger (2004).
The tethered configuration of the EGF receptor extracellular domain exerts only a limited control of receptor function.
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CR1/CR2 interactions modulate the functions of the cell surface epidermal growth factor receptor.
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Targeted therapies in oncology: in the crosshairs or at the crossroads?
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Signaling multiplex of the epidermal growth factor receptor.
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15235591 J.Kniazeff, A.S.Bessis, D.Maurel, H.Ansanay, L.Prézeau, and J.P.Pin (2004).
Closed state of both binding domains of homodimeric mGlu receptors is required for full activity.
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GW domains of the Listeria monocytogenes invasion protein InlB are required for potentiation of Met activation.
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Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex.
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PDB code: 1s78
15070899 M.Kim, H.Yang, S.K.Kim, P.A.Reche, R.S.Tirabassi, R.E.Hussey, Y.Chishti, J.G.Rheinwald, T.J.Morehead, T.Zech, I.K.Damon, R.M.Welsh, and E.L.Reinherz (2004).
Biochemical and functional analysis of smallpox growth factor (SPGF) and anti-SPGF monoclonal antibodies.
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15576039 M.Landau, S.J.Fleishman, and N.Ben-Tal (2004).
A putative mechanism for downregulation of the catalytic activity of the EGF receptor via direct contact between its kinase and C-terminal domains.
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15215236 M.Offterdinger, V.Georget, A.Girod, and P.I.Bastiaens (2004).
Imaging phosphorylation dynamics of the epidermal growth factor receptor.
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14993704 N.Kulahin, C.Kasper, M.Gajhede, V.Berezin, E.Bock, and J.S.Kastrup (2004).
Expression, crystallization and preliminary X-ray analysis of extracellular modules of the neural cell-adhesion molecules NCAM and L1.
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14732694 P.Klein, D.Mattoon, M.A.Lemmon, and J.Schlessinger (2004).
A structure-based model for ligand binding and dimerization of EGF receptors.
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Suppression of the biological activities of the epidermal growth factor (EGF)-like domain by the heparin-binding domain of heparin-binding EGF-like Growth Factor.
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Regulation of the Drosophila epidermal growth factor-ligand vein is mediated by multiple domains.
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15075331 T.G.Johns, T.E.Adams, J.R.Cochran, N.E.Hall, P.A.Hoyne, M.J.Olsen, Y.S.Kim, J.Rothacker, E.C.Nice, F.Walker, G.Ritter, A.A.Jungbluth, L.J.Old, C.W.Ward, A.W.Burgess, K.D.Wittrup, and A.M.Scott (2004).
Identification of the epitope for the epidermal growth factor receptor-specific monoclonal antibody 806 reveals that it preferentially recognizes an untethered form of the receptor.
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14744244 T.Holbro, and N.E.Hynes (2004).
ErbB receptors: directing key signaling networks throughout life.
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15231819 Y.X.Fan, L.Wong, T.B.Deb, and G.R.Johnson (2004).
Ligand regulates epidermal growth factor receptor kinase specificity: activation increases preference for GAB1 and SHC versus autophosphorylation sites.
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An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors.
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An evolutionary and structural perspective on T cell antigen receptor function.
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12734179 C.Couturier, and R.Jockers (2003).
Activation of the leptin receptor by a ligand-induced conformational change of constitutive receptor dimers.
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Inhibition of heregulin signaling by an aptamer that preferentially binds to the oligomeric form of human epidermal growth factor receptor-3.
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Selective formation of ErbB-2/ErbB-3 heterodimers depends on the ErbB-3 affinity of epidermal growth factor-like ligands.
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14632199 C.Stove, V.Stove, L.Derycke, V.Van Marck, M.Mareel, and M.Bracke (2003).
The heregulin/human epidermal growth factor receptor as a new growth factor system in melanoma with multiple ways of deregulation.
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14528000 E.Gherardi, M.E.Youles, R.N.Miguel, T.L.Blundell, L.Iamele, J.Gough, A.Bandyopadhyay, G.Hartmann, and P.J.Butler (2003).
Functional map and domain structure of MET, the product of the c-met protooncogene and receptor for hepatocyte growth factor/scatter factor.
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Cholesterol depletion results in site-specific increases in epidermal growth factor receptor phosphorylation due to membrane level effects. Studies with cholesterol enantiomers.
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Topological requirements and signaling properties of T cell-activating, anti-CD28 antibody superagonists.
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Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab.
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PDB codes: 1n8y 1n8z
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The EGF receptor family--multiple roles in proliferation, differentiation, and neoplasia with an emphasis on HER4.
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12667445 J.Greenwald, J.Groppe, P.Gray, E.Wiater, W.Kwiatkowski, W.Vale, and S.Choe (2003).
The BMP7/ActRII extracellular domain complex provides new insights into the cooperative nature of receptor assembly.
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PDB codes: 1lx5 1lxi
12620237 K.M.Ferguson, M.B.Berger, J.M.Mendrola, H.S.Cho, D.J.Leahy, and M.A.Lemmon (2003).
EGF activates its receptor by removing interactions that autoinhibit ectodomain dimerization.
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PDB code: 1nql
12791136 M.P.Machner, S.Frese, W.D.Schubert, V.Orian-Rousseau, E.Gherardi, J.Wehland, H.H.Niemann, and D.W.Heinz (2003).
Aromatic amino acids at the surface of InlB are essential for host cell invasion by Listeria monocytogenes.
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12869572 M.Wingens, T.Walma, H.van Ingen, C.Stortelers, J.E.van Leeuwen, E.J.van Zoelen, and G.W.Vuister (2003).
Structural analysis of an epidermal growth factor/transforming growth factor-alpha chimera with unique ErbB binding specificity.
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PDB code: 1p9j
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12695504 S.Schenk, E.Hintermann, M.Bilban, N.Koshikawa, C.Hojilla, R.Khokha, and V.Quaranta (2003).
Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution.
  J Cell Biol, 161, 197-209.  
12620236 T.P.Garrett, N.M.McKern, M.Lou, T.C.Elleman, T.E.Adams, G.O.Lovrecz, M.Kofler, R.N.Jorissen, E.C.Nice, A.W.Burgess, and C.W.Ward (2003).
The crystal structure of a truncated ErbB2 ectodomain reveals an active conformation, poised to interact with other ErbB receptors.
  Mol Cell, 11, 495-505.
PDB code: 2a91
14708119 W.S.Hlavacek, J.R.Faeder, M.L.Blinov, A.S.Perelson, and B.Goldstein (2003).
The complexity of complexes in signal transduction.
  Biotechnol Bioeng, 84, 783-794.  
12731890 Y.Zhen, R.M.Caprioli, and J.V.Staros (2003).
Characterization of glycosylation sites of the epidermal growth factor receptor.
  Biochemistry, 42, 5478-5492.  
12196540 J.Stamos, M.X.Sliwkowski, and C.Eigenbrot (2002).
Structure of the epidermal growth factor receptor kinase domain alone and in complex with a 4-anilinoquinazoline inhibitor.
  J Biol Chem, 277, 46265-46272.
PDB codes: 1m14 1m17
12297049 T.P.Garrett, N.M.McKern, M.Lou, T.C.Elleman, T.E.Adams, G.O.Lovrecz, H.J.Zhu, F.Walker, M.J.Frenkel, P.A.Hoyne, R.N.Jorissen, E.C.Nice, A.W.Burgess, and C.W.Ward (2002).
Crystal structure of a truncated epidermal growth factor receptor extracellular domain bound to transforming growth factor alpha.
  Cell, 110, 763-773.
PDB code: 1mox
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