Crystal structure of the Ig1 domain of the neural cell adhesion molecule NCAM2 displays domain swapping.

Kim Krighaar Rasmussen; Nikolaj Kulahin; Ole Kristensen; Jens-Christian N Poulsen; Bent W Sigurskjold; Jette S Kastrup; Vladimir Berezin; Elisabeth Bock; Peter S Walmod; Michael Gajhede

doi:10.1016/j.jmb.2008.07.084

Crystal structure of the Ig1 domain of the neural cell adhesion molecule NCAM2 displays domain swapping.

Kim Krighaar Rasmussen, Nikolaj Kulahin, Ole Kristensen, Jens-Christian N Poulsen, Bent W Sigurskjold, Jette S Kastrup, Vladimir Berezin, Elisabeth Bock, Peter S Walmod, Michael Gajhede

7 Citations (Scopus)

Abstract

The crystal structure of the first immunoglobulin (Ig1) domain of neural cell adhesion molecule 2 (NCAM2/OCAM/RNCAM) is presented at a resolution of 2.7 A. NCAM2 is a member of the immunoglobulin superfamily of cell adhesion molecules (IgCAMs). In the structure, two Ig domains interact by domain swapping, as the two N-terminal beta-strands are interchanged. beta-Strand swapping at the terminal domain is the accepted mechanism of homophilic interactions amongst the cadherins, another class of CAMs, but it has not been observed within the IgCAM superfamily. Gel-filtration chromatography demonstrated the ability of NCAM2 Ig1 to form dimers in solution. Taken together, these observations suggest that beta-strand swapping could have a role in the molecular mechanism of homophilic binding for NCAM2.

Original language	English
Journal	Journal of Molecular Biology
Volume	382
Issue number	5
Pages (from-to)	1113-20
Number of pages	7
ISSN	0022-2836
DOIs	https://doi.org/10.1016/j.jmb.2008.07.084
Publication status	Published - 2008

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@article{f7bd61508b2411dd9c20000ea68e967b,

title = "Crystal structure of the Ig1 domain of the neural cell adhesion molecule NCAM2 displays domain swapping.",

abstract = "The crystal structure of the first immunoglobulin (Ig1) domain of neural cell adhesion molecule 2 (NCAM2/OCAM/RNCAM) is presented at a resolution of 2.7 A. NCAM2 is a member of the immunoglobulin superfamily of cell adhesion molecules (IgCAMs). In the structure, two Ig domains interact by domain swapping, as the two N-terminal beta-strands are interchanged. beta-Strand swapping at the terminal domain is the accepted mechanism of homophilic interactions amongst the cadherins, another class of CAMs, but it has not been observed within the IgCAM superfamily. Gel-filtration chromatography demonstrated the ability of NCAM2 Ig1 to form dimers in solution. Taken together, these observations suggest that beta-strand swapping could have a role in the molecular mechanism of homophilic binding for NCAM2.",

author = "Rasmussen, {Kim Krighaar} and Nikolaj Kulahin and Ole Kristensen and Poulsen, {Jens-Christian N} and Sigurskjold, {Bent W} and Kastrup, {Jette S} and Vladimir Berezin and Elisabeth Bock and Walmod, {Peter S} and Michael Gajhede",

year = "2008",

doi = "10.1016/j.jmb.2008.07.084",

language = "English",

volume = "382",

pages = "1113--20",

journal = "Journal of Molecular Biology",

issn = "0022-2836",

publisher = "Academic Press",

number = "5",

}

TY - JOUR

T1 - Crystal structure of the Ig1 domain of the neural cell adhesion molecule NCAM2 displays domain swapping.

AU - Rasmussen, Kim Krighaar

AU - Kulahin, Nikolaj

AU - Kristensen, Ole

AU - Poulsen, Jens-Christian N

AU - Sigurskjold, Bent W

AU - Kastrup, Jette S

AU - Berezin, Vladimir

AU - Bock, Elisabeth

AU - Walmod, Peter S

AU - Gajhede, Michael

PY - 2008

Y1 - 2008

N2 - The crystal structure of the first immunoglobulin (Ig1) domain of neural cell adhesion molecule 2 (NCAM2/OCAM/RNCAM) is presented at a resolution of 2.7 A. NCAM2 is a member of the immunoglobulin superfamily of cell adhesion molecules (IgCAMs). In the structure, two Ig domains interact by domain swapping, as the two N-terminal beta-strands are interchanged. beta-Strand swapping at the terminal domain is the accepted mechanism of homophilic interactions amongst the cadherins, another class of CAMs, but it has not been observed within the IgCAM superfamily. Gel-filtration chromatography demonstrated the ability of NCAM2 Ig1 to form dimers in solution. Taken together, these observations suggest that beta-strand swapping could have a role in the molecular mechanism of homophilic binding for NCAM2.

AB - The crystal structure of the first immunoglobulin (Ig1) domain of neural cell adhesion molecule 2 (NCAM2/OCAM/RNCAM) is presented at a resolution of 2.7 A. NCAM2 is a member of the immunoglobulin superfamily of cell adhesion molecules (IgCAMs). In the structure, two Ig domains interact by domain swapping, as the two N-terminal beta-strands are interchanged. beta-Strand swapping at the terminal domain is the accepted mechanism of homophilic interactions amongst the cadherins, another class of CAMs, but it has not been observed within the IgCAM superfamily. Gel-filtration chromatography demonstrated the ability of NCAM2 Ig1 to form dimers in solution. Taken together, these observations suggest that beta-strand swapping could have a role in the molecular mechanism of homophilic binding for NCAM2.

U2 - 10.1016/j.jmb.2008.07.084

DO - 10.1016/j.jmb.2008.07.084

M3 - Journal article

C2 - 18706912

SN - 0022-2836

VL - 382

SP - 1113

EP - 1120

JO - Journal of Molecular Biology

JF - Journal of Molecular Biology

IS - 5

ER -

Crystal structure of the Ig1 domain of the neural cell adhesion molecule NCAM2 displays domain swapping.

Abstract

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