The structure of human apolipoprotein A-IV as revealed by stable isotope-assisted cross-linking, molecular dynamics, and small angle x-ray scattering
Apolipoprotein (apo) A-IV plays important roles in dietary lipid and glucose metabolism, and
knowledge of its structure is required to fully understand the molecular basis of these
functions. However, typical of the entire class of exchangeable apolipoproteins, its dynamic
nature and affinity for lipid has posed challenges to traditional high resolution structural
approaches. We previously reported an x-ray crystal structure of a dimeric truncation mutant
of apoA-IV, which showed a unique helix-swapping molecular interface. Unfortunately, the …
knowledge of its structure is required to fully understand the molecular basis of these
functions. However, typical of the entire class of exchangeable apolipoproteins, its dynamic
nature and affinity for lipid has posed challenges to traditional high resolution structural
approaches. We previously reported an x-ray crystal structure of a dimeric truncation mutant
of apoA-IV, which showed a unique helix-swapping molecular interface. Unfortunately, the …
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