Structure and Sequence Analyses of Clustered Protocadherins Reveal Antiparallel Interactions that Mediate Homophilic Specificity.

@article{Nicoludis2015StructureAS,
  title={Structure and Sequence Analyses of Clustered Protocadherins Reveal Antiparallel Interactions that Mediate Homophilic Specificity.},
  author={John M. Nicoludis and Sze-Yi Lau and Charlotta P I Sch{\"a}rfe and Debora S. Marks and Wilhelm Andreas Weihofen and Rachelle Gaudet},
  journal={Structure},
  year={2015},
  volume={23 11},
  pages={2087-98}
}
Clustered protocadherin (Pcdh) proteins mediate dendritic self-avoidance in neurons via specific homophilic interactions in their extracellular cadherin (EC) domains. We determined crystal structures of EC1-EC3, containing the homophilic specificity-determining region, of two mouse clustered Pcdh isoforms (PcdhγA1 and PcdhγC3) to investigate the nature of the homophilic interaction. Within the crystal lattices, we observe antiparallel interfaces consistent with a role in trans cell-cell contact… CONTINUE READING

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