Structural basis of cell-cell adhesion by NCAM

Research output: Contribution to journalJournal articleResearchpeer-review

Standard

Structural basis of cell-cell adhesion by NCAM. / Kasper, C; Rasmussen, H; Kastrup, Jette Sandholm Jensen; Ikemizu, S; Jones, E Y; Berezin, V; Bock, E; Larsen, I K.

In: Nature Structural and Molecular Biology, Vol. 7, No. 5, 2000, p. 389-393.

Research output: Contribution to journalJournal articleResearchpeer-review

Harvard

Kasper, C, Rasmussen, H, Kastrup, JSJ, Ikemizu, S, Jones, EY, Berezin, V, Bock, E & Larsen, IK 2000, 'Structural basis of cell-cell adhesion by NCAM', Nature Structural and Molecular Biology, vol. 7, no. 5, pp. 389-393. https://doi.org/10.1038/75165

APA

Kasper, C., Rasmussen, H., Kastrup, J. S. J., Ikemizu, S., Jones, E. Y., Berezin, V., ... Larsen, I. K. (2000). Structural basis of cell-cell adhesion by NCAM. Nature Structural and Molecular Biology, 7(5), 389-393. https://doi.org/10.1038/75165

Vancouver

Kasper C, Rasmussen H, Kastrup JSJ, Ikemizu S, Jones EY, Berezin V et al. Structural basis of cell-cell adhesion by NCAM. Nature Structural and Molecular Biology. 2000;7(5):389-393. https://doi.org/10.1038/75165

Author

Kasper, C ; Rasmussen, H ; Kastrup, Jette Sandholm Jensen ; Ikemizu, S ; Jones, E Y ; Berezin, V ; Bock, E ; Larsen, I K. / Structural basis of cell-cell adhesion by NCAM. In: Nature Structural and Molecular Biology. 2000 ; Vol. 7, No. 5. pp. 389-393.

Bibtex

@article{13124fd074c811dbbee902004c4f4f50,
title = "Structural basis of cell-cell adhesion by NCAM",
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.",
keywords = "Amino Acid Sequence, Animals, Binding Sites, Calcium, Cell Adhesion, Crystallography, X-Ray, Dimerization, Heparin, Hydrogen Bonding, Immunoglobulins, Models, Molecular, Molecular Sequence Data, Neural Cell Adhesion Molecules, Protein Binding, Protein Structure, Secondary, Protein Structure, Tertiary, Rats, Sequence Alignment, Structure-Activity Relationship",
author = "C Kasper and H Rasmussen and Kastrup, {Jette Sandholm Jensen} and S Ikemizu and Jones, {E Y} and V Berezin and E Bock and Larsen, {I K}",
year = "2000",
doi = "10.1038/75165",
language = "English",
volume = "7",
pages = "389--393",
journal = "Nature Structural and Molecular Biology",
issn = "1545-9993",
publisher = "nature publishing group",
number = "5",

}

RIS

TY - JOUR

T1 - Structural basis of cell-cell adhesion by NCAM

AU - Kasper, C

AU - Rasmussen, H

AU - Kastrup, Jette Sandholm Jensen

AU - Ikemizu, S

AU - Jones, E Y

AU - Berezin, V

AU - Bock, E

AU - Larsen, I K

PY - 2000

Y1 - 2000

N2 - 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.

AB - 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.

KW - Amino Acid Sequence

KW - Animals

KW - Binding Sites

KW - Calcium

KW - Cell Adhesion

KW - Crystallography, X-Ray

KW - Dimerization

KW - Heparin

KW - Hydrogen Bonding

KW - Immunoglobulins

KW - Models, Molecular

KW - Molecular Sequence Data

KW - Neural Cell Adhesion Molecules

KW - Protein Binding

KW - Protein Structure, Secondary

KW - Protein Structure, Tertiary

KW - Rats

KW - Sequence Alignment

KW - Structure-Activity Relationship

U2 - 10.1038/75165

DO - 10.1038/75165

M3 - Journal article

C2 - 10802736

VL - 7

SP - 389

EP - 393

JO - Nature Structural and Molecular Biology

JF - Nature Structural and Molecular Biology

SN - 1545-9993

IS - 5

ER -

ID: 177814