ABCA1 p.Ala1950Val
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PMID: 18776170
[PubMed]
Vaughan AM et al: "ABCA1 mutants reveal an interdependency between lipid export function, apoA-I binding activity, and Janus kinase 2 activation."
No.
Sentence
Comment
50
We also generated an artificial mutation in the Walker A motif of NBD2 (A1950V) that corresponds to the A937V mutation in NBD1.
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ABCA1 p.Ala1950Val 18776170:50:72
status: NEW82 This activation was nearly abolished in cells expressing all mutants except two (W590S and A1950V), which are the same two mutants that have the highest ability to cross-link apoA-I (Fig. 2E).
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ABCA1 p.Ala1950Val 18776170:82:91
status: NEW93 The two most severe mutations, which reduced apoA-I-mediated lipid efflux to less than 20% of normal, were located in the first extracellular loop (Q597R) and the ATP binding site (A937V).
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ABCA1 p.Ala1950Val 18776170:93:72
status: NEW94 Interestingly, the equivalent mutation in the ATP binding site of NBD2 (A1950V) had only a modest impairment of ABCA1 function, suggesting that the ATP binding activity of NBD1 is more critical for function than that of NBD2 or that these mutations have different effects on protein conformation.
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ABCA1 p.Ala1950Val 18776170:94:72
status: NEW138 and A1950V, which also had near-normal apoA-I cross-linking activity.
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ABCA1 p.Ala1950Val 18776170:138:4
status: NEW137 and A1950V, which also had near-normal apoA-I cross-linking activity.
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ABCA1 p.Ala1950Val 18776170:137:4
status: NEW