TY - JOUR
T1 - Meta-Analysis of the Expansion in the Field of Structural Biology of ABC Transporters
AU - Kim, Soomi
AU - Bajaj, Teena
AU - Chabon, Cole
AU - Tablante, Eric
AU - Kulchinskaya, Tatyana
AU - Moon, Tae Seok
AU - Bajaj, Ruchika
N1 - Publisher Copyright:
Copyright © 2022 Soomi Kim et al.
PY - 2022
Y1 - 2022
N2 - ABC transporters are molecular machines which power the solute transport using ATP hydrolysis. The structural biology of ABC transporters has been exploding for the last few years, and this study explores timelines and trends for various attributes such as structural tools, resolution, fold, sources, and group leaders. This study also evidences the significance of mammalian expression systems, advancements in structural biology tools, and the developing interest of group leaders across the world in the remarkably progressing field. The field started in 2002 and bloomed in 2016, and COVID years were really productive to the field. Specifically, the study explores 337 structures of 58 unique ABC transporters deposited in the PDB database from which P-glycoprotein has the largest number of structures. Approximately, 62% of total structures are determined at the resolution of 3-4 Å and 53% of structures belong to fold IV type. With progressive advancements in the field, the field is shifting from prokaryotic to eukaryotic sources and X-ray crystallography to cryoelectron microscopy. In the nutshell, this study uniquely provides the detailed snapshot of the field of structural biology of ABC transporters with real-time data.
AB - ABC transporters are molecular machines which power the solute transport using ATP hydrolysis. The structural biology of ABC transporters has been exploding for the last few years, and this study explores timelines and trends for various attributes such as structural tools, resolution, fold, sources, and group leaders. This study also evidences the significance of mammalian expression systems, advancements in structural biology tools, and the developing interest of group leaders across the world in the remarkably progressing field. The field started in 2002 and bloomed in 2016, and COVID years were really productive to the field. Specifically, the study explores 337 structures of 58 unique ABC transporters deposited in the PDB database from which P-glycoprotein has the largest number of structures. Approximately, 62% of total structures are determined at the resolution of 3-4 Å and 53% of structures belong to fold IV type. With progressive advancements in the field, the field is shifting from prokaryotic to eukaryotic sources and X-ray crystallography to cryoelectron microscopy. In the nutshell, this study uniquely provides the detailed snapshot of the field of structural biology of ABC transporters with real-time data.
UR - http://www.scopus.com/inward/record.url?scp=85140364534&partnerID=8YFLogxK
U2 - 10.34133/2022/9806979
DO - 10.34133/2022/9806979
M3 - Review article
AN - SCOPUS:85140364534
SN - 2693-1257
VL - 2022
JO - BioDesign Research
JF - BioDesign Research
M1 - 9806979
ER -