5JDP

E73V mutant of the human voltage-dependent anion channel

Summary for 5JDP

• Entry DOI: 10.2210/pdb5jdp/pdb
• NMR Information: BMRB: 30065
• Descriptor: Voltage-dependent anion-selective channel protein 1 (1 entity in total)
• Functional Keywords: membrane protein, structure refinement, sparse data, protein dynamics, relaxation
• Biological source: Homo sapiens (Human)
• Total number of polymer chains: 1
• Total formula weight: 30977.70

Authors

Jaremko, M.,Jaremko, L.,Villinger, S.,Schmidt, C.,Giller, K.,Griesinger, C.,Becker, S.,Zweckstetter, M. (deposition date: 2016-04-17, release date: 2016-08-10, Last modification date: 2024-06-19)

Primary citation

Jaremko, M.,Villinger, S.,Schmidt, C.D.,Griesinger, C.,Becker, S.,Zweckstetter, M.
High-Resolution NMR Determination of the Dynamic Structure of Membrane Proteins.
Angew.Chem.Int.Ed.Engl., 55:10518-10521, 2016

PubMed Abstract: (15) N spin-relaxation rates are demonstrated to provide critical information about the long-range structure and internal motions of membrane proteins. Combined with an improved calculation method, the relaxation-rate-derived structure of the 283-residue human voltage-dependent anion channel revealed an anisotropically shaped barrel with a rigidly attached N-terminal helix. Our study thus establishes an NMR spectroscopic approach to determine the structure and dynamics of mammalian membrane proteins at high accuracy and resolution.

PubMed: 27461260
DOI: 10.1002/anie.201602639

Experimental method

SOLUTION NMR