Fei Li1, Pascal F Egea2, Alex J Vecchio3, Ignacio Asial4, Meghna Gupta5, Joana Paulino5, Ruchika Bajaj6, Miles Sasha Dickinson5, Shelagh Ferguson-Miller7, Brian C Monk8, Robert M Stroud9. 1. Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, USA; Department of Neurology, University of California San Francisco, San Francisco, California, USA. 2. Department of Biological Chemistry, School of Medicine, University of California Los Angeles, Los Angeles, California, USA. 3. Department of Biochemistry, University of Nebraska-Lincoln, Lincoln, Nebraska, USA. 4. DotBio Pte. Ltd, Singapore, Singapore. 5. Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, USA. 6. Department of Bioengineering and Therapeutic Sciences, University of California San Francisco, San Francisco, California, USA. 7. Department of Biochemistry and Molecular Biology, Michigan State University, East Lansing, Michigan, USA. 8. Sir John Walsh Research Institute and Department of Oral Sciences, University of Otago, North Dunedin, Dunedin, New Zealand. 9. Department of Biochemistry and Biophysics, University of California San Francisco, San Francisco, California, USA. Electronic address: stroud@msg.ucsf.edu.
Abstract
Biological membranes define the boundaries of cells and compartmentalize the chemical and physical processes required for life. Many biological processes are carried out by proteins embedded in or associated with such membranes. Determination of membrane protein (MP) structures at atomic or near-atomic resolution plays a vital role in elucidating their structural and functional impact in biology. This endeavor has determined 1198 unique MP structures as of early 2021. The value of these structures is expanded greatly by deposition of their three-dimensional (3D) coordinates into the Protein Data Bank (PDB) after the first atomic MP structure was elucidated in 1985. Since then, free access to MP structures facilitates broader and deeper understanding of MPs, which provides crucial new insights into their biological functions. Here we highlight the structural and functional biology of representative MPs and landmarks in the evolution of new technologies, with insights into key developments influenced by the PDB in magnifying their impact.
Biological membranes define the boundaries of cells and compn class="Chemical">artmentalize the chemical and physical processes required for life. Many biological processes are carried out by proteins embedded in or associated with such membranes. Determination of membrane protein (MP) structures at atomic or near-atomic resolution plays a vital role in elucidating their structural and functional impact in biology. This endeavor has determined 1198 unique MP structures as of early 2021. The value of these structures is expanded greatly by deposition of their three-dimensional (3D) coordinates into the Protein Data Bank (PDB) after the first atomic MP structure was elucidated in 1985. Since then, free access to MP structures facilitates broader and deeper understanding of MPs, which provides crucial new insights into their biological functions. Here we highlight the structural and functional biology of representative MPs and landmarks in the evolution of new technologies, with insights into key developments influenced by the PDB in magnifying their impact.
Keywords:
bioenergetics; channel; drug discovery; lipid mimetics; membrane protein; membrane protein biogenesis; protein design; receptor; structure-function; transmembrane transport
Authors: Alba Nin-Hill; Nicolas Pierre Friedrich Mueller; Carla Molteni; Carme Rovira; Mercedes Alfonso-Prieto Journal: Int J Mol Sci Date: 2021-11-08 Impact factor: 5.923
Authors: Adrian H Kopf; Odette Lijding; Barend O W Elenbaas; Martijn C Koorengevel; Justyna M Dobruchowska; Cornelis A van Walree; J Antoinette Killian Journal: Biomacromolecules Date: 2022-01-07 Impact factor: 6.988
Authors: Ivan Gushchin; Vladimir A Aleksenko; Philipp Orekhov; Ivan M Goncharov; Vera V Nazarenko; Oleg Semenov; Alina Remeeva; Valentin Gordeliy Journal: Int J Mol Sci Date: 2021-05-31 Impact factor: 5.923