5OEK

Putative active dimeric state of GHR transmembrane domain

Summary for 5OEK

• Entry DOI: 10.2210/pdb5oek/pdb
• NMR Information: BMRB: 34160
• Descriptor: Growth hormone receptor (1 entity in total)
• Functional Keywords: dimer, ghr, growth hormone receptor, homodimer, human, receptor, transmembrane domain, 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: 2017-07-08, 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

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: 29571748
DOI: 10.1016/j.bbagen.2018.03.022

Experimental method

SOLUTION NMR