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Structural basis of cell-cell adhesion by NCAM.

Kasper C, Rasmussen H, Kastrup JS, Ikemizu S, Jones EY, Berezin V, Bock E, Larsen IK
Nat Struct Biol 7 389-93 (2000)
Cited: 68 times
EuropePMC logo PMID: 10802736

Abstract

The neural cell adhesion molecule NCAM, a member of the immunoglobulin superfamily, mediates cell-cell recognition and adhesion via a homophilic interaction. NCAM plays a key role during development and regeneration of the nervous system and is involved in synaptic plasticity associated with memory and learning. The 1.85 A crystal structure of the two N-terminal extracellular domains of NCAM reported here provides a structural basis for the homophilic interaction. The molecular packing of the two-domain structure reveals a cross shaped antiparallel dimer, and provides fundamental insight into trans-cellular recognition mediated by NCAM.

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  41. Historical Article Special issue dedicated to Elisabeth Bock. Berezin V. Neurochem. Res. 38 1089-1091 (2013)
  42. Tyro3, Axl, and Mertk receptors differentially participate in platelet activation and thrombus formation. Zhou J, Yang A, Wang Y, Chen F, Zhao Z, Davra V, Suzuki-Inoue K, Ozaki Y, Birge RB, Lu Q, Wu Y. Cell Commun. Signal 16 98 (2018)
  43. WITHDRAWN: Special Issue Honoring Dr. Elisabeth Bock. Berezin V. Neurochem Res (2008)
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Related citations provided by authors (1)

  1. Expression, crystallization and preliminary X-ray analysis of the two amino-terminal Ig domains of the neural cell adhesion molecule (NCAM).. Kasper C, Rasmussen H, Berezin V, Bock E, Larsen IK Acta Crystallogr D Biol Crystallogr 55 1598-600 (1999)

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