ABCMdb

PMID: 26295388

Paolini A, Baldassarre A, Del Gaudio I, Masotti A
Structural Features of the ATP-Binding Cassette (ABC) Transporter ABCA3.
Int J Mol Sci. 2015 Aug 19;16(8):19631-44. doi: 10.3390/ijms160819631., [PubMed]

Sentences

No. Mutations Sentence Comment

49 ABCA3 p.Asn568Asp One of these in vitro studies demonstrated that the p.N568D mutation in ABCA3 impairs choline-phospholipids uptake into intracellular vesicles in lung adenocarcinoma A549 cells [25] and primary AT2 cells [26]. Login to comment 50 ABCA3 p.Asn568Asp Moreover, in WT cells` ultrastructural images confirmed the regular formation of lamellar bodies, whereas in the p.N568D mutant the formation of these multilamellar vesicles has not been observed. Login to comment 111 ABCA3 p.Glu292Val ABCA3 p.Leu1553Pro ABCA3 p.Trp1142* ABCA3 p.Glu690Lys ABCA3 p.Tyr1515* ABCA3 p.Arg1333Gly In particular, we focused on the following mutations: p.E292V, p.E690K, p.R1333G, p.W1142X, p.Y1515X, and p.L1553P. Login to comment 113 ABCA3 p.Glu292Val The p.E292V mutation, one of the most frequently observed in humans [61], is localized in a loop very close to the terminal part of the transporter channel and we may hypothesize that this amino acid is involved in ATP or substrate binding. Login to comment 114 ABCA3 p.Leu1553Pro ABCA3 p.Glu690Lys ABCA3 p.Tyr1515* p.E690K reside in the NBD1, whereas p.Y1515X and p.L1553P are localized in the NBD2. Login to comment 116 ABCA3 p.Trp1142* ABCA3 p.Arg1333Gly More difficult is to hypothesize a role for p.W1142X and p.R1333G both residing in b1;-helices of the transmembrane domain 2 (TMD2). Login to comment