2N5S
Spatial structure of EGFR transmembrane and juxtamembrane domains in DPC micelles
Summary for 2N5S
| Entry DOI | 10.2210/pdb2n5s/pdb |
| NMR Information | BMRB: 25729 |
| Descriptor | Epidermal growth factor receptor (1 entity in total) |
| Functional Keywords | transmembrane, transferase |
| Biological source | Homo sapiens (human) |
| Cellular location | Cell membrane; Single-pass type I membrane protein. Isoform 2: Secreted: P00533 |
| Total number of polymer chains | 1 |
| Total formula weight | 5979.34 |
| Authors | Mineev, K.,Bocharov, E.,Bocharova, O.,Arseniev, A. (deposition date: 2015-07-27, release date: 2015-10-14, Last modification date: 2024-05-15) |
| Primary citation | Mineev, K.S.,Panova, S.V.,Bocharova, O.V.,Bocharov, E.V.,Arseniev, A.S. The Membrane Mimetic Affects the Spatial Structure and Mobility of EGFR Transmembrane and Juxtamembrane Domains. Biochemistry, 54:6295-6298, 2015 Cited by PubMed Abstract: The epidermal growth factor receptor (EGFR) is one of the most extensively studied receptor tyrosine kinases, as it is involved in a wide range of cellular processes and severe diseases. Recent works reveal that the single-helix transmembrane domains and cytoplasmic juxtamembrane regions play an important role in the receptor activation process. Here we present the results of our investigation of the spatial structure and mobility of the EGFR transmembrane domain and juxtamembrane regions in various membranelike environments, which shed light on the effects of the membrane physical properties and composition on the behavior of the juxtamembrane domain. PubMed: 26440883DOI: 10.1021/acs.biochem.5b00851 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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