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PDBsum entry 2evt
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Lipid transport
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PDB id
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2evt
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References listed in PDB file
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Key reference
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Title
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The liganding of glycolipid transfer protein is controlled by glycolipid acyl structure.
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Authors
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L.Malinina,
M.L.Malakhova,
A.T.Kanack,
M.Lu,
R.Abagyan,
R.E.Brown,
D.J.Patel.
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Ref.
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Plos Biol, 2006,
4,
e362.
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PubMed id
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Abstract
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Glycosphingolipids (GSLs) play major roles in cellular growth and development.
Mammalian glycolipid transfer proteins (GLTPs) are potential regulators of cell
processes mediated by GSLs and display a unique architecture among lipid
binding/transfer proteins. The GLTP fold represents a novel membrane
targeting/interaction domain among peripheral proteins. Here we report crystal
structures of human GLTP bound to GSLs of diverse acyl chain length,
unsaturation, and sugar composition. Structural comparisons show a highly
conserved anchoring of galactosyl- and lactosyl-amide headgroups by the GLTP
recognition center. By contrast, acyl chain chemical structure and occupancy of
the hydrophobic tunnel dictate partitioning between sphingosine-in and
newly-observed sphingosine-out ligand-binding modes. The structural insights,
combined with computed interaction propensity distributions, suggest a concerted
sequence of events mediated by GLTP conformational changes during GSL transfer
to and/or from membranes, as well as during GSL presentation and/or transfer to
other proteins.
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