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PDBsum entry 1m6b
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protein ligands Protein-protein interface(s) links
Signaling protein, transferase PDB id
1m6b

 

 

 

 

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JSmol PyMol  
Contents
Protein chains
549 a.a. *
584 a.a. *
Ligands
NAG-NAG ×2
NAG ×13
SO4
Waters ×85
* Residue conservation analysis
PDB id:
1m6b
Name: Signaling protein, transferase
Title: Structure of the her3 (erbb3) extracellular domain
Structure: Receptor protein-tyrosine kinase erbb-3. Chain: a, b. Fragment: extracellular domain. Synonym: growth factor receptor extracellular domain. C-erbb3. Tyrosine kinase-type cell surface receptor her3. Epidermal growth factor receptor. V-erb-b2 erythroblastic leukemia viral oncogene homolog. Engineered: yes
Source: Homo sapiens. Human. Organism_taxid: 9606. Expressed in: cricetulus griseus. Expression_system_taxid: 10029. Expression_system_cell_line: lec1. Expression_system_tissue: ovary cells.
Resolution:
2.60Å     R-factor:   0.238     R-free:   0.294
Authors: D.J.Leahy,H.-S.Cho
Key ref:
H.S.Cho and D.J.Leahy (2002). Structure of the extracellular region of HER3 reveals an interdomain tether. Science, 297, 1330-1333. PubMed id: 12154198 DOI: 10.1126/science.1074611
Date:
15-Jul-02     Release date:   02-Aug-02    
PROCHECK
Go to PROCHECK summary
 Headers
 References

Protein chain
Pfam   ArchSchema ?
P21860  (ERBB3_HUMAN) -  Receptor tyrosine-protein kinase erbB-3 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1342 a.a.
549 a.a.*
Protein chain
Pfam   ArchSchema ?
P21860  (ERBB3_HUMAN) -  Receptor tyrosine-protein kinase erbB-3 from Homo sapiens
Seq:
Struc: 		 
Seq:
Struc: 		 
Seq:
Struc: 		1342 a.a.
584 a.a.*
Key:    PfamA domain  Secondary structure  CATH domain
* PDB and UniProt seqs differ at 6 residue positions (black crosses)

 Enzyme reactions 
   Enzyme class: Chains A, B: E.C.2.7.10.1  - receptor protein-tyrosine kinase.
[IntEnz]   [ExPASy]   [KEGG]   [BRENDA]
      Reaction: L-tyrosyl-[protein] + ATP = O-phospho-L-tyrosyl-[protein] + ADP + H+
L-tyrosyl-[protein]
 +
ATP
Bound ligand (Het Group name = NAG)
matches with 47.62% similarity 		= O-phospho-L-tyrosyl-[protein]
 + ADP
 + H(+)
Molecule diagrams generated from .mol files obtained from the KEGG ftp site

 

 
    Added reference    
 
 
DOI no: 10.1126/science.1074611 Science 297:1330-1333 (2002)
PubMed id: 12154198  
 
 
Structure of the extracellular region of HER3 reveals an interdomain tether.
H.S.Cho, D.J.Leahy.
 
  ABSTRACT  
 
We have determined the 2.6 angstrom crystal structure of the entire extracellular region of human HER3 (ErbB3), a member of the epidermal growth factor receptor (EGFR) family. The structure consists of four domains with structural homology to domains found in the type I insulin-like growth factor receptor. The HER3 structure reveals a contact between domains II and IV that constrains the relative orientations of ligand-binding domains and provides a structural basis for understanding both multiple-affinity forms of EGFRs and conformational changes induced in the receptor by ligand binding during signaling. These results also suggest new therapeutic approaches to modulating the behavior of members of the EGFR family.
 
  Selected figure(s)  
 
Figure 2.
Fig. 2. The domain II/IV contact. (A) Side chains of residues that mediate contacts between domain II (green) and domain IV (red) are shown. Hydrogen bonds and salt bridges are indicated by dashed lines. This figure was made with MOLSCRIPT (36). (B) Alignment of human ErbB receptor sequences from the domain II/IV contact regions. Residues with direct contacts to one another in sHER3 are highlighted in similar colors. Pro593 and Phe^595 of HER2, which fail to conserve the pattern of contact residues, are underlined. 		Figure 3.
Fig. 3. Surface representations of sHER3 and EGF (32). sHER3 is rotated ~180° about a vertical axis relative to its orientation in Fig. 1A. EGF and the sites in sHER3 (Y104 and V333) homologous to the sites in HER1 to which EGF cross-links (30, 31) are in red. Domains I to IV and the domain II/IV connection are labeled. This figure was made with the program GRASP (37).
 
  The above figures are reprinted by permission from the AAAs: Science (2002, 297, 1330-1333) copyright 2002.  
  Figures were selected by an automated process.  

Literature references that cite this PDB file's key reference

  PubMed id Reference
22785351 Y.Yarden, and G.Pines (2012).
The ERBB network: at last, cancer therapy meets systems biology.
  Nat Rev Cancer, 12, 553-563.  
21288302 F.Troise, M.Monti, A.Merlino, F.Cozzolino, C.Fedele, I.R.Krauss, F.Sica, P.Pucci, G.D'Alessio, and C.De Lorenzo (2011).
A novel ErbB2 epitope targeted by human antitumor immunoagents.
  FEBS J, 278, 1156-1166.  
20966750 H.Tsujioka, F.Yotsumoto, S.Hikita, T.Ueda, M.Kuroki, and S.Miyamoto (2011).
Targeting the heparin-binding epidermal growth factor-like growth factor in ovarian cancer therapy.
  Curr Opin Obstet Gynecol, 23, 24-30.  
21822280 L.Z.Mi, C.Lu, Z.Li, N.Nishida, T.Walz, and T.A.Springer (2011).
Simultaneous visualization of the extracellular and cytoplasmic domains of the epidermal growth factor receptor.
  Nat Struct Mol Biol, 18, 984-989.  
20723758 D.Alvarado, D.E.Klein, and M.A.Lemmon (2010).
Structural basis for negative cooperativity in growth factor binding to an EGF receptor.
  Cell, 142, 568-579.
PDB codes: 3ltf 3ltg
20430953 E.Witsch, M.Sela, and Y.Yarden (2010).
Roles for growth factors in cancer progression.
  Physiology (Bethesda), 25, 85.  
20432069 J.H.Bae, and J.Schlessinger (2010).
Asymmetric tyrosine kinase arrangements in activation or autophosphorylation of receptor tyrosine kinases.
  Mol Cells, 29, 443-448.  
21119106 L.Chen, J.Placone, L.Novicky, and K.Hristova (2010).
The extracellular domain of fibroblast growth factor receptor 3 inhibits ligand-independent dimerization.
  Sci Signal, 3, ra86.  
20642809 S.Cho, K.Kim, Y.J.Kim, J.K.Lee, Y.S.Cho, J.Y.Lee, B.G.Han, H.Kim, J.Ott, and T.Park (2010).
Joint identification of multiple genetic variants via elastic-net variable selection in a genome-wide association analysis.
  Ann Hum Genet, 74, 416-428.  
19518076 C.Qiu, M.K.Tarrant, T.Boronina, P.A.Longo, J.M.Kavran, R.N.Cole, P.A.Cole, and D.J.Leahy (2009).
In vitro enzymatic characterization of near full length EGFR in activated and inhibited states.
  Biochemistry, 48, 6624-6632.  
19718021 D.Alvarado, D.E.Klein, and M.A.Lemmon (2009).
ErbB2 resembles an autoinhibited invertebrate epidermal growth factor receptor.
  Nature, 461, 287-291.
PDB code: 3i2t
19536107 J.Baselga, and S.M.Swain (2009).
Novel anticancer targets: revisiting ERBB2 and discovering ERBB3.
  Nat Rev Cancer, 9, 463-475.  
19564416 J.Kalinina, S.A.Byron, H.P.Makarenkova, S.K.Olsen, A.V.Eliseenkova, W.J.Larochelle, M.Dhanabal, S.Blais, D.M.Ornitz, L.A.Day, T.A.Neubert, P.M.Pollock, and M.Mohammadi (2009).
Homodimerization controls the fibroblast growth factor 9 subfamily's receptor binding and heparan sulfate-dependent diffusion in the extracellular matrix.
  Mol Cell Biol, 29, 4663-4678.
PDB code: 3f1r
  20357902 K.L.Carraway, and G.A.Kozloski (2009).
Conformational changes in receptor tyrosine kinase signaling: an ErbB garden of delights.
  F1000 Biol Rep, 1, 1-4.  
18992239 K.R.Schmitz, and K.M.Ferguson (2009).
Interaction of antibodies with ErbB receptor extracellular regions.
  Exp Cell Res, 315, 659-670.  
19486684 L.Chen, M.Merzlyakov, T.Cohen, Y.Shai, and K.Hristova (2009).
Energetics of ErbB1 transmembrane domain dimerization in lipid bilayers.
  Biophys J, 96, 4622-4630.  
19038249 M.A.Lemmon (2009).
Ligand-induced ErbB receptor dimerization.
  Exp Cell Res, 315, 638-648.  
20477507 M.Yamauchi, and N.Gotoh (2009).
Theme: oncology--molecular mechanisms determining the efficacy of EGF receptor-specific tyrosine kinase inhibitors help to identify biomarker candidates.
  Biomark Med, 3, 139-151.  
20007378 N.Jura, Y.Shan, X.Cao, D.E.Shaw, and J.Kuriyan (2009).
Structural analysis of the catalytically inactive kinase domain of the human EGF receptor 3.
  Proc Natl Acad Sci U S A, 106, 21608-21613.
PDB code: 3kex
19245710 N.Yutin, M.Y.Wolf, Y.I.Wolf, and E.V.Koonin (2009).
The origins of phagocytosis and eukaryogenesis.
  Biol Direct, 4, 9.  
  19048033 P.Jin, J.Zhang, M.Beryt, L.Turin, C.Brdlik, Y.Feng, X.Bai, J.Liu, B.Jorgensen, and H.M.Shepard (2009).
Rational optimization of a bispecific ligand trap targeting EGF receptor family ligands.
  Mol Med, 15, 11-20.  
18761339 R.Bose, and X.Zhang (2009).
The ErbB kinase domain: structural perspectives into kinase activation and inhibition.
  Exp Cell Res, 315, 649-658.  
19289058 S.E.Telesco, and R.Radhakrishnan (2009).
Atomistic insights into regulatory mechanisms of the HER2 tyrosine kinase domain: a molecular dynamics study.
  Biophys J, 96, 2321-2334.  
19376231 S.O'Connor, E.Li, B.S.Majors, L.He, J.Placone, D.Baycin, M.J.Betenbaugh, and K.Hristova (2009).
Increased expression of the integral membrane protein ErbB2 in Chinese hamster ovary cells expressing the anti-apoptotic gene Bcl-xL.
  Protein Expr Purif, 67, 41-47.  
19878579 Y.Zhang, L.Opresko, H.Shankaran, W.B.Chrisler, H.S.Wiley, and H.Resat (2009).
HER/ErbB receptor interactions and signaling patterns in human mammary epithelial cells.
  BMC Cell Biol, 10, 78.  
18334220 C.Qiu, M.K.Tarrant, S.H.Choi, A.Sathyamurthy, R.Bose, S.Banjade, A.Pal, W.G.Bornmann, M.A.Lemmon, P.A.Cole, and D.J.Leahy (2008).
Mechanism of activation and inhibition of the HER4/ErbB4 kinase.
  Structure, 16, 460-467.
PDB codes: 3bbt 3bbw 3bce
18798529 G.K.Dy, and A.A.Adjei (2008).
Systemic cancer therapy: evolution over the last 60 years.
  Cancer, 113, 1857-1887.  
18394559 J.Schmiedel, A.Blaukat, S.Li, T.Knöchel, and K.M.Ferguson (2008).
Matuzumab binding to EGFR prevents the conformational rearrangement required for dimerization.
  Cancer Cell, 13, 365-373.
PDB codes: 3c08 3c09
18773073 K.Buac, D.E.Watkins-Chow, S.K.Loftus, D.M.Larson, A.Incao, G.Gibney, and W.J.Pavan (2008).
A Sox10 expression screen identifies an amino acid essential for Erbb3 function.
  PLoS Genet, 4, e1000177.  
18573086 K.M.Ferguson (2008).
Structure-based view of epidermal growth factor receptor regulation.
  Annu Rev Biophys, 37, 353-373.  
18771282 L.Z.Mi, M.J.Grey, N.Nishida, T.Walz, C.Lu, and T.A.Springer (2008).
Functional and structural stability of the epidermal growth factor receptor in detergent micelles and phospholipid nanodiscs.
  Biochemistry, 47, 10314-10323.  
18259690 M.J.Wieduwilt, and M.M.Moasser (2008).
The epidermal growth factor receptor family: biology driving targeted therapeutics.
  Cell Mol Life Sci, 65, 1566-1584.  
18031935 M.Landau, and N.Ben-Tal (2008).
Dynamic equilibrium between multiple active and inactive conformations explains regulation and oncogenic mutations in ErbB receptors.
  Biochim Biophys Acta, 1785, 12-31.  
19045821 M.Y.Hsieh, S.Yang, M.A.Raymond-Stinz, S.Steinberg, D.G.Vlachos, W.Shu, B.Wilson, and J.S.Edwards (2008).
Stochastic simulations of ErbB homo and heterodimerisation: potential impacts of receptor conformational state and spatial segregation.
  IET Syst Biol, 2, 256-272.  
18365190 O.Samna Soumana, N.Garnier, and M.Genest (2008).
Insight into the recognition patterns of the ErbB receptor family transmembrane domains: heterodimerization models through molecular dynamics search.
  Eur Biophys J, 37, 851-864.  
17890389 S.E.Webb, S.K.Roberts, S.R.Needham, C.J.Tynan, D.J.Rolfe, M.D.Winn, D.T.Clarke, R.Barraclough, and M.L.Martin-Fernandez (2008).
Single-molecule imaging and fluorescence lifetime imaging microscopy show different structures for high- and low-affinity epidermal growth factor receptors in A431 cells.
  Biophys J, 94, 803-819.  
18275813 S.Li, P.Kussie, and K.M.Ferguson (2008).
Structural basis for EGF receptor inhibition by the therapeutic antibody IMC-11F8.
  Structure, 16, 216-227.
PDB codes: 3b2u 3b2v
17280834 C.W.Ward, M.C.Lawrence, V.A.Streltsov, T.E.Adams, and N.M.McKern (2007).
The insulin and EGF receptor structures: new insights into ligand-induced receptor activation.
  Trends Biochem Sci, 32, 129-137.  
17508401 D.J.Riese, R.M.Gallo, and J.Settleman (2007).
Mutational activation of ErbB family receptor tyrosine kinases: insights into mechanisms of signal transduction and tumorigenesis.
  Bioessays, 29, 558-565.  
17314037 E.M.Bublil, and Y.Yarden (2007).
The EGF receptor family: spearheading a merger of signaling and therapeutics.
  Curr Opin Cell Biol, 19, 124-134.  
17701904 G.Narkis, R.Ofir, E.Manor, D.Landau, K.Elbedour, and O.S.Birk (2007).
Lethal congenital contractural syndrome type 2 (LCCS2) is caused by a mutation in ERBB3 (Her3), a modulator of the phosphatidylinositol-3-kinase/Akt pathway.
  Am J Hum Genet, 81, 589-595.  
17671639 H.Zhang, A.Berezov, Q.Wang, G.Zhang, J.Drebin, R.Murali, and M.I.Greene (2007).
ErbB receptors: from oncogenes to targeted cancer therapies.
  J Clin Invest, 117, 2051-2058.  
18075577 J.Kuriyan, and D.Eisenberg (2007).
The origin of protein interactions and allostery in colocalization.
  Nature, 450, 983-990.  
17697999 J.P.Dawson, Z.Bu, and M.A.Lemmon (2007).
Ligand-induced structural transitions in ErbB receptor extracellular domains.
  Structure, 15, 942-954.  
17274834 R.Landgraf (2007).
HER2 therapy. HER2 (ERBB2): functional diversity from structurally conserved building blocks.
  Breast Cancer Res, 9, 202.  
17553674 W.Liu, K.Zscheppang, S.Murray, H.C.Nielsen, and C.E.Dammann (2007).
The ErbB4 receptor in fetal rat lung fibroblasts and epithelial type II cells.
  Biochim Biophys Acta, 1772, 737-747.  
17155902 A.Yasmeen, T.A.Bismar, and A.E.Al Moustafa (2006).
ErbB receptors and epithelial-cadherin-catenin complex in human carcinomas.
  Future Oncol, 2, 765-781.  
16983832 B.S.Hendriks, J.Cook, J.M.Burke, J.M.Beusmans, D.A.Lauffenburger, and D.de Graaf (2006).
Computational modelling of ErbB family phosphorylation dynamics in response to transforming growth factor alpha and heregulin indicates spatial compartmentation of phosphatase activity.
  Syst Biol (Stevenage), 153, 22-33.  
16865534 C.Sweeney, J.K.Miller, D.L.Shattuck, and K.L.Carraway (2006).
ErbB receptor negative regulatory mechanisms: implications in cancer.
  J Mammary Gland Biol Neoplasia, 11, 89-99.  
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.
  BMC Bioinformatics, 7, 38.  
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.
  Breast Cancer Res Treat, 95, 17-27.  
17026767 R.A.Stein, and J.V.Staros (2006).
Insights into the evolution of the ErbB receptor family and their ligands from sequence analysis.
  BMC Evol Biol, 6, 79.  
16788977 S.Kamath, and J.K.Buolamwini (2006).
Targeting EGFR and HER-2 receptor tyrosine kinases for cancer drug discovery and development.
  Med Res Rev, 26, 569-594.  
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.
  Cell, 125, 1137-1149.
PDB codes: 2gs2 2gs6 2gs7
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.
  EMBO J, 25, 4215-4222.  
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.
  Proteins, 59, 742-756.  
16288303 F.Cappuzzo, L.Toschi, I.Domenichini, S.Bartolini, G.L.Ceresoli, E.Rossi, V.Ludovini, A.Cancellieri, E.Magrini, L.Bemis, W.A.Franklin, L.Crino, P.A.Bunn, F.R.Hirsch, and M.Varella-Garcia (2005).
HER3 genomic gain and sensitivity to gefitinib in advanced non-small-cell lung cancer patients.
  Br J Cancer, 93, 1334-1340.  
16107719 J.P.Dawson, M.B.Berger, C.C.Lin, J.Schlessinger, M.A.Lemmon, and K.M.Ferguson (2005).
Epidermal growth factor receptor dimerization and activation require ligand-induced conformational changes in the dimer interface.
  Mol Cell Biol, 25, 7734-7742.  
15864276 N.E.Hynes, and H.A.Lane (2005).
ERBB receptors and cancer: the complexity of targeted inhibitors.
  Nat Rev Cancer, 5, 341-354.  
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.
  Biopolymers, 77, 184-197.  
15596490 P.Bagossi, G.Horváth, G.Vereb, J.Szöllösi, and J.Tözsér (2005).
Molecular modeling of nearly full-length ErbB2 receptor.
  Biophys J, 88, 1354-1363.  
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.
  Proc Natl Acad Sci U S A, 102, 15024-15029.
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.
  Cancer Cell, 7, 301-311.
PDB codes: 1yy8 1yy9
15094157 A.Bennasroune, A.Gardin, D.Aunis, G.Crémel, and P.Hubert (2004).
Tyrosine kinase receptors as attractive targets of cancer therapy.
  Crit Rev Oncol Hematol, 50, 23-38.  
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.
  Proc Natl Acad Sci U S A, 101, 923-928.  
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.
  Nat Struct Mol Biol, 11, 706-713.  
15352163 J.R.Peterson, and E.A.Golemis (2004).
Autoinhibited proteins as promising drug targets.
  J Cell Biochem, 93, 68-73.  
15093539 M.C.Franklin, K.D.Carey, F.F.Vajdos, D.J.Leahy, A.M.de Vos, and M.X.Sliwkowski (2004).
Insights into ErbB signaling from the structure of the ErbB2-pertuzumab complex.
  Cancer Cell, 5, 317-328.
PDB code: 1s78
14732694 P.Klein, D.Mattoon, M.A.Lemmon, and J.Schlessinger (2004).
A structure-based model for ligand binding and dimerization of EGF receptors.
  Proc Natl Acad Sci U S A, 101, 929-934.  
14744244 T.Holbro, and N.E.Hynes (2004).
ErbB receptors: directing key signaling networks throughout life.
  Annu Rev Pharmacol Toxicol, 44, 195-217.  
14527402 A.W.Burgess, H.S.Cho, C.Eigenbrot, K.M.Ferguson, T.P.Garrett, D.J.Leahy, M.A.Lemmon, M.X.Sliwkowski, C.W.Ward, and S.Yokoyama (2003).
An open-and-shut case? Recent insights into the activation of EGF/ErbB receptors.
  Mol Cell, 12, 541-552.  
12604783 B.H.Luo, T.A.Springer, and J.Takagi (2003).
Stabilizing the open conformation of the integrin headpiece with a glycan wedge increases affinity for ligand.
  Proc Natl Acad Sci U S A, 100, 2403-2408.  
12874383 C.H.Chen, G.A.Chernis, V.Q.Hoang, and R.Landgraf (2003).
Inhibition of heregulin signaling by an aptamer that preferentially binds to the oligomeric form of human epidermal growth factor receptor-3.
  Proc Natl Acad Sci U S A, 100, 9226-9231.  
12817993 C.J.Witton (2003).
Structure of HER receptors and intracellular localisation of downstream effector elements gives insight into mechanism of tumour growth promotion.
  Breast Cancer Res, 5, 206-207.  
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.
  J Invest Dermatol, 121, 802-812.  
12610629 H.S.Cho, K.Mason, K.X.Ramyar, A.M.Stanley, S.B.Gabelli, D.W.Denney, and D.J.Leahy (2003).
Structure of the extracellular region of HER2 alone and in complex with the Herceptin Fab.
  Nature, 421, 756-760.
PDB codes: 1n8y 1n8z
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.
  Mol Cell, 11, 507-517.
PDB code: 1nql
12605220 M.X.Sliwkowski (2003).
Ready to partner.
  Nat Struct Biol, 10, 158-159.  
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
12360255 P.De Meyts, and J.Whittaker (2002).
Structural biology of insulin and IGF1 receptors: implications for drug design.
  Nat Rev Drug Discov, 1, 769-783.  
The most recent references are shown first. Citation data come partly from CiteXplore and partly from an automated harvesting procedure. Note that this is likely to be only a partial list as not all journals are covered by either method. However, we are continually building up the citation data so more and more references will be included with time. Where a reference describes a PDB structure, the PDB codes are shown on the right.

 

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