5OHD
Putative inactive (dormant) dimeric state of GHR transmembrane domain
Summary for 5OHD
Entry DOI | 10.2210/pdb5ohd/pdb |
Related | 5OEK |
NMR Information | BMRB: 34164 |
Descriptor | Growth hormone receptor (1 entity in total) |
Functional Keywords | dimer, ghr, growth hormone receptor, homodimer, human, receptor, transmembrane domain, jak2 tyrosine kinase, membrane protein |
Biological source | Homo sapiens (Human) |
Total number of polymer chains | 2 |
Total formula weight | 10290.26 |
Authors | Lesovoy, D.M.,Bocharov, E.V.,Bocharova, O.V.,Urban, A.S.,Arseniev, A.S. (deposition date: 2017-07-15, release date: 2018-04-11, Last modification date: 2024-07-03) |
Primary citation | Bocharov, E.V.,Lesovoy, D.M.,Bocharova, O.V.,Urban, A.S.,Pavlov, K.V.,Volynsky, P.E.,Efremov, R.G.,Arseniev, A.S. Structural basis of the signal transduction via transmembrane domain of the human growth hormone receptor. Biochim. Biophys. Acta, 1862:1410-1420, 2018 Cited by PubMed Abstract: Prior studies of the human growth hormone receptor (GHR) revealed a distinct role of spatial rearrangements of its dimeric transmembrane domain in signal transduction across membrane. Detailed structural information obtained in the present study allowed elucidating the bases of such rearrangement and provided novel insights into receptor functioning. PubMed: 29571748DOI: 10.1016/j.bbagen.2018.03.022 PDB entries with the same primary citation |
Experimental method | SOLUTION NMR |
Structure validation
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