The neural cell adhesion molecule NCAM, a member of the immunoglobulin supe
rfamily, mediates cell-cell recognition and adhesion via a hemophilic inter
action. NCAM plays a key role during development and regeneration of the ne
rvous system and is involved in synaptic plasticity associated with memory
and learning. The 1.85 Angstrom crystal structure of the two N-terminal ext
racellular domains of NCAM reported here provides a structural basis for th
e hemophilic interaction. The molecular packing of the two-domain structure
reveals a cross shaped antiparallel dimer, and provides fundamental insigh
t into trans-cellular recognition mediated by NCAM.