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1RQU
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BU of 1rqu by Molmil
NMR structure of L7 dimer from E.coli
Descriptor: 50S ribosomal protein L7/L12
Authors:Bocharov, E.V, Sobol, A.G, Pavlov, K.V, Korzhnev, D.M, Jaravine, V.A, Gudkov, A.T, Arseniev, A.S.
Deposit date:2003-12-07
Release date:2004-03-02
Last modified:2022-03-02
Method:SOLUTION NMR
Cite:From structure and dynamics of protein L7/L12 to molecular switching in ribosome.
J.Biol.Chem., 279, 2004
1RQS
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BU of 1rqs by Molmil
NMR structure of C-terminal domain of ribosomal protein L7 from E.coli
Descriptor: 50S ribosomal protein L7/L12
Authors:Bocharov, E.V, Sobol, A.G, Pavlov, K.V, Korzhnev, D.M, Jaravine, V.A, Gudkov, A.T, Arseniev, A.S.
Deposit date:2003-12-07
Release date:2004-03-02
Last modified:2022-03-02
Method:SOLUTION NMR
Cite:From structure and dynamics of protein L7/L12 to molecular switching in ribosome.
J.Biol.Chem., 279, 2004
1RQT
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BU of 1rqt by Molmil
NMR structure of dimeric N-terminal domain of ribosomal protein L7 from E.coli
Descriptor: 50S ribosomal protein L7/L12
Authors:Bocharov, E.V, Sobol, A.G, Pavlov, K.V, Korzhnev, D.M, Jaravine, V.A, Gudkov, A.T, Arseniev, A.S.
Deposit date:2003-12-07
Release date:2004-03-02
Last modified:2022-03-02
Method:SOLUTION NMR
Cite:From structure and dynamics of protein L7/L12 to molecular switching in ribosome.
J.Biol.Chem., 279, 2004
1RQV
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BU of 1rqv by Molmil
Spatial model of L7 dimer from E.coli with one hinge region in helical state
Descriptor: 50S ribosomal protein L7/L12
Authors:Bocharov, E.V, Sobol, A.G, Pavlov, K.V, Korzhnev, D.M, Jaravine, V.A, Gudkov, A.T, Arseniev, A.S.
Deposit date:2003-12-07
Release date:2004-03-02
Last modified:2022-03-02
Method:SOLUTION NMR
Cite:From structure and dynamics of protein L7/L12 to molecular switching in ribosome
J.Biol.Chem., 279, 2004
5LV6
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BU of 5lv6 by Molmil
N-terminal motif dimerization of EGFR transmembrane domain in bicellar environment
Descriptor: Epidermal growth factor receptor
Authors:Bragin, P, Bocharov, E, Mineev, K, Bocharova, O, Arseniev, A.
Deposit date:2016-09-12
Release date:2017-04-05
Last modified:2023-06-14
Method:SOLUTION NMR
Cite:The Conformation of the Epidermal Growth Factor Receptor Transmembrane Domain Dimer Dynamically Adapts to the Local Membrane Environment.
Biochemistry, 56, 2017
5OEK
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BU of 5oek by Molmil
Putative active dimeric state of GHR transmembrane domain
Descriptor: Growth hormone receptor
Authors:Lesovoy, D.M, Bocharov, E.V, Bocharova, O.V, Urban, A.S, Arseniev, A.S.
Deposit date:2017-07-08
Release date:2018-04-11
Last modified:2023-06-14
Method:SOLUTION NMR
Cite:Structural basis of the signal transduction via transmembrane domain of the human growth hormone receptor.
Biochim. Biophys. Acta, 1862, 2018
5OHD
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BU of 5ohd by Molmil
Putative inactive (dormant) dimeric state of GHR transmembrane domain
Descriptor: Growth hormone receptor
Authors:Lesovoy, D.M, Bocharov, E.V, Bocharova, O.V, Urban, A.S, Arseniev, A.S.
Deposit date:2017-07-15
Release date:2018-04-11
Last modified:2023-06-14
Method:SOLUTION NMR
Cite:Structural basis of the signal transduction via transmembrane domain of the human growth hormone receptor.
Biochim. Biophys. Acta, 1862, 2018
2J5D
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BU of 2j5d by Molmil
NMR structure of BNIP3 transmembrane domain in lipid bicelles
Descriptor: BCL2/ADENOVIRUS E1B 19 KDA PROTEIN-INTERACTING PROTEIN 3
Authors:Bocharov, E.V, Pustovalova, Y.E, Volynsky, P.E, Maslennikov, I.V, Goncharuk, M.V, Ermolyuk, Y.S, Arseniev, A.S.
Deposit date:2006-09-14
Release date:2007-04-17
Last modified:2020-01-15
Method:SOLUTION NMR
Cite:Unique dimeric structure of BNip3 transmembrane domain suggests membrane permeabilization as a cell death trigger.
J. Biol. Chem., 282, 2007
2M0B
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BU of 2m0b by Molmil
Homodimeric transmembrane domain of the human receptor tyrosine kinase ErbB1 (EGFR, HER1) in micelles
Descriptor: Epidermal growth factor receptor
Authors:Lesovoy, D.M, Bocharov, E.V, Pustovalova, Y.E, Bocharova, O.V, Arseniev, A.S.
Deposit date:2012-10-24
Release date:2013-10-30
Last modified:2019-06-26
Method:SOLUTION NMR
Cite:Alternative packing of EGFR transmembrane domain suggests that protein-lipid interactions underlie signal conduction across membrane.
Biochim. Biophys. Acta, 1858, 2016

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