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PDBsum entry 3p3y
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Cell adhesion
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PDB id
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3p3y
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References listed in PDB file
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Key reference
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Title
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Homophilic adhesion mechanism of neurofascin, A member of the l1 family of neural cell adhesion molecules.
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Authors
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H.Liu,
P.J.Focia,
X.He.
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Ref.
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J Biol Chem, 2011,
286,
797-805.
[DOI no: ]
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PubMed id
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Abstract
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The L1 family neural cell adhesion molecules play key roles in specifying the
formation and remodeling of the neural network, but their homophilic interaction
that mediates adhesion is not well understood. We report two crystal structures
of a dimeric form of the headpiece of neurofascin, an L1 family member. The four
N-terminal Ig-like domains of neurofascin form a horseshoe shape, akin to
several other immunoglobulin superfamily cell adhesion molecules such as
hemolin, axonin, and Dscam. The neurofascin dimer, captured in two crystal forms
with independent packing patterns, reveals a pair of horseshoes in
trans-synaptic adhesion mode. The adhesion interaction is mediated mostly by the
second Ig-like domain, which features an intermolecular β-sheet formed by the
joining of two individual GFC β-sheets and a large but loosely packed
hydrophobic cluster. Mutagenesis combined with gel filtration assays suggested
that the side chain hydrogen bonds at the intermolecular β-sheet are essential
for the homophilic interaction and that the residues at the hydrophobic cluster
play supplementary roles. Our structures reveal a conserved homophilic adhesion
mode for the L1 family and also shed light on how the pathological mutations of
L1 affect its structure and function.
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