Structural and functional diversity calls for a new classification of ABC transporters.
Structural and functional diversity calls for a new classification of ABC transporters.
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DOI:
10.1002/1873-3468.13935
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发表时间:
2020-12
期刊:
影响因子:
3.5
通讯作者:
Tampé R
中科院分区:
文献类型:
--
作者:
Thomas C;Aller SG;Beis K;Carpenter EP;Chang G;Chen L;Dassa E;Dean M;Duong Van Hoa F;Ekiert D;Ford R;Gaudet R;Gong X;Holland IB;Huang Y;Kahne DK;Kato H;Koronakis V;Koth CM;Lee Y;Lewinson O;Lill R;Martinoia E;Murakami S;Pinkett HW;Poolman B;Rosenbaum D;Sarkadi B;Schmitt L;Schneider E;Shi Y;Shyng SL;Slotboom DJ;Tajkhorshid E;Tieleman DP;Ueda K;Váradi A;Wen PC;Yan N;Zhang P;Zheng H;Zimmer J;Tampé R
Members of the ATP-binding cassette (ABC) transporter superfamily translocate a broad spectrum of chemically diverse substrates. While their eponymous ATP-binding cassette in the nucleotide-binding domains (NBDs) is highly conserved, their transmembrane domains (TMDs) forming the translocation pathway exhibit distinct folds and topologies, suggesting that during evolution the ancient motor domains were combined with different transmembrane mechanical systems to orchestrate a variety of cellular processes. In recent years, it has become increasingly evident that the distinct TMD folds are best suited to categorize the multitude of ABC transporters. We therefore propose a new ABC transporter classification that is based on structural homology in the TMDs.
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