Structural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion molecule

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Structural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion molecule. / Kulahin, Nikolaj; Kristensen, Ole; Rasmussen, Kim K; Olsen, Lars; Rydberg, Patrik; Vestergaard, Bente; Kastrup, Jette Sandholm; Berezin, Vladimir; Bock, Elisabeth; Walmod, Peter Schledermann; Gajhede, Michael.

In: Structure, Vol. 19, No. 2, 09.02.2011, p. 203-211.

Research output: Contribution to journal › Journal article › Research › peer-review

Harvard

Kulahin, N, Kristensen, O, Rasmussen, KK, Olsen, L, Rydberg, P, Vestergaard, B, Kastrup, JS, Berezin, V, Bock, E, Walmod, PS & Gajhede, M 2011, 'Structural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion molecule', Structure, vol. 19, no. 2, pp. 203-211. https://doi.org/10.1016/j.str.2010.12.014

APA

Kulahin, N., Kristensen, O., Rasmussen, K. K., Olsen, L., Rydberg, P., Vestergaard, B., Kastrup, J. S., Berezin, V., Bock, E., Walmod, P. S., & Gajhede, M. (2011). Structural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion molecule. Structure, 19(2), 203-211. https://doi.org/10.1016/j.str.2010.12.014

Vancouver

Kulahin N, Kristensen O, Rasmussen KK, Olsen L, Rydberg P, Vestergaard B et al. Structural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion molecule. Structure. 2011 Feb 9;19(2):203-211. https://doi.org/10.1016/j.str.2010.12.014

Author

Kulahin, Nikolaj ; Kristensen, Ole ; Rasmussen, Kim K ; Olsen, Lars ; Rydberg, Patrik ; Vestergaard, Bente ; Kastrup, Jette Sandholm ; Berezin, Vladimir ; Bock, Elisabeth ; Walmod, Peter Schledermann ; Gajhede, Michael. / Structural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion molecule. In: Structure. 2011 ; Vol. 19, No. 2. pp. 203-211.

Bibtex

@article{9fa3b20806494f47969d5b85cec23157,

title = "Structural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion molecule",

abstract = "The ectodomain of olfactory cell adhesion molecule (OCAM/NCAM2/RNCAM) consists of five immunoglobulin (Ig) domains (IgI-V), followed by two fibronectin-type 3 (Fn3) domains (Fn3I-II). A complete structural model of the entire ectodomain of human OCAM has been assembled from crystal structures of six recombinant proteins corresponding to different regions of the ectodomain. The model is the longest experimentally based composite structural model of an entire IgCAM ectodomain. It displays an essentially linear arrangement of IgI-V, followed by bends between IgV and Fn3I and between Fn3I and Fn3II. Proteins containing IgI-IgII domains formed stable homodimers in solution and in crystals. Dimerization could be disrupted in vitro by mutations in the dimer interface region. In conjunction with the bent ectodomain conformation, which can position IgI-V parallel with the cell surface, the IgI-IgII dimerization enables OCAM-mediated trans-interactions with an intercellular distance of about 20 nm, which is consistent with that observed in synapses.",

keywords = "Faculty of Health and Medical Sciences",

author = "Nikolaj Kulahin and Ole Kristensen and Rasmussen, {Kim K} and Lars Olsen and Patrik Rydberg and Bente Vestergaard and Kastrup, {Jette Sandholm} and Vladimir Berezin and Elisabeth Bock and Walmod, {Peter Schledermann} and Michael Gajhede",

year = "2011",

month = feb,

day = "9",

doi = "10.1016/j.str.2010.12.014",

language = "English",

volume = "19",

pages = "203--211",

journal = "Structure",

issn = "0969-2126",

publisher = "Cell Press",

number = "2",

}

RIS

TY - JOUR

T1 - Structural model and trans-interaction of the entire ectodomain of the olfactory cell adhesion molecule

AU - Kulahin, Nikolaj

AU - Kristensen, Ole

AU - Rasmussen, Kim K

AU - Olsen, Lars

AU - Rydberg, Patrik

AU - Vestergaard, Bente

AU - Kastrup, Jette Sandholm

AU - Berezin, Vladimir

AU - Bock, Elisabeth

AU - Walmod, Peter Schledermann

AU - Gajhede, Michael

PY - 2011/2/9

Y1 - 2011/2/9

N2 - The ectodomain of olfactory cell adhesion molecule (OCAM/NCAM2/RNCAM) consists of five immunoglobulin (Ig) domains (IgI-V), followed by two fibronectin-type 3 (Fn3) domains (Fn3I-II). A complete structural model of the entire ectodomain of human OCAM has been assembled from crystal structures of six recombinant proteins corresponding to different regions of the ectodomain. The model is the longest experimentally based composite structural model of an entire IgCAM ectodomain. It displays an essentially linear arrangement of IgI-V, followed by bends between IgV and Fn3I and between Fn3I and Fn3II. Proteins containing IgI-IgII domains formed stable homodimers in solution and in crystals. Dimerization could be disrupted in vitro by mutations in the dimer interface region. In conjunction with the bent ectodomain conformation, which can position IgI-V parallel with the cell surface, the IgI-IgII dimerization enables OCAM-mediated trans-interactions with an intercellular distance of about 20 nm, which is consistent with that observed in synapses.

AB - The ectodomain of olfactory cell adhesion molecule (OCAM/NCAM2/RNCAM) consists of five immunoglobulin (Ig) domains (IgI-V), followed by two fibronectin-type 3 (Fn3) domains (Fn3I-II). A complete structural model of the entire ectodomain of human OCAM has been assembled from crystal structures of six recombinant proteins corresponding to different regions of the ectodomain. The model is the longest experimentally based composite structural model of an entire IgCAM ectodomain. It displays an essentially linear arrangement of IgI-V, followed by bends between IgV and Fn3I and between Fn3I and Fn3II. Proteins containing IgI-IgII domains formed stable homodimers in solution and in crystals. Dimerization could be disrupted in vitro by mutations in the dimer interface region. In conjunction with the bent ectodomain conformation, which can position IgI-V parallel with the cell surface, the IgI-IgII dimerization enables OCAM-mediated trans-interactions with an intercellular distance of about 20 nm, which is consistent with that observed in synapses.

KW - Faculty of Health and Medical Sciences

U2 - 10.1016/j.str.2010.12.014

DO - 10.1016/j.str.2010.12.014

M3 - Journal article

C2 - 21300289

VL - 19

SP - 203

EP - 211

JO - Structure

JF - Structure

SN - 0969-2126

IS - 2

ER -

ID: 33000065

Faculty of Law