2JWA
ErbB2 transmembrane segment dimer spatial structure
Summary for 2JWA
| Entry DOI | 10.2210/pdb2jwa/pdb |
| Descriptor | Receptor tyrosine-protein kinase erbB-2 (1 entity in total) |
| Functional Keywords | transmembrane helix dimer, erbb2, protein kinase receptor membrane domain, atp-binding, glycoprotein, nucleotide-binding, phosphorylation, polymorphism, transferase, tyrosine-protein kinase |
| Biological source | Homo sapiens (human) |
| Cellular location | Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cytoplasm. Isoform 3: Cytoplasm: P04626 |
| Total number of polymer chains | 2 |
| Total formula weight | 9469.61 |
| Authors | Mineev, K.S.,Bocharov, E.V.,Arseniev, A.S. (deposition date: 2007-10-09, release date: 2008-01-22, Last modification date: 2024-05-29) |
| Primary citation | Bocharov, E.V.,Mineev, K.S.,Volynsky, P.E.,Ermolyuk, Y.S.,Tkach, E.N.,Sobol, A.G.,Chupin, V.V.,Kirpichnikov, M.P.,Efremov, R.G.,Arseniev, A.S. Spatial Structure of the Dimeric Transmembrane Domain of the Growth Factor Receptor ErbB2 Presumably Corresponding to the Receptor Active State J.Biol.Chem., 283:6950-6956, 2008 Cited by PubMed Abstract: Proper lateral dimerization of the transmembrane domains of receptor tyrosine kinases is required for biochemical signal transduction across the plasma membrane. The spatial structure of the dimeric transmembrane domain of the growth factor receptor ErbB2 embedded into lipid bicelles was obtained by solution NMR, followed by molecular dynamics relaxation in an explicit lipid bilayer. ErbB2 transmembrane segments associate in a right-handed alpha-helical bundle through the N-terminal tandem GG4-like motif Thr652-X3-Ser656-X3-Gly660, providing an explanation for the pathogenic power of some oncogenic mutations. PubMed: 18178548DOI: 10.1074/jbc.M709202200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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