The crystal structure of the CmABCB1 G132V mutant, which favors the outward‐facing state, reveals the mechanism of the pivotal joint between TM1 and TM3

CmABCB1 is a homologue of human P‐glycoprotein, which extrudes various substrates by iterative cycles of conformational changes between the inward‐ and outward‐facing states. Comparison of the inward‐ and outward‐facing structures of CmABCB1 suggested that pivotal joints in the transmembrane domain...

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Veröffentlicht in:	Protein science 2021-05, Vol.30 (5), p.1064-1071
Hauptverfasser:	Matsuoka, Keita, Nakatsu, Toru, Kato, Hiroaki
Format:	Artikel
Sprache:	eng
Schlagworte:	ABC transporter Adenosine triphosphatase Amino Acid Substitution ATP Binding Cassette Transporter, Subfamily B, Member 1 - chemistry ATP Binding Cassette Transporter, Subfamily B, Member 1 - genetics Crystal structure Crystallography, X-Ray Domains Glycoproteins Helices Homology multidrug transporter Mutants Mutation Mutation, Missense Nucleotides Protein Structure Reports Protein Structure, Secondary P‐glycoprotein Rhodophyta - chemistry Rhodophyta - genetics Steric hindrance Substrates Valine X‐ray crystallography
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