Structural basis for the activation of FGFR by NCAM

Artur Kochoyan; Flemming Poulsen; Vladimir Berezin; Elisabeth Marianne Bock; Vladislav Kiselyov

doi:10.1110/ps.035964.108

Structural basis for the activation of FGFR by NCAM

Artur Kochoyan, Flemming Poulsen, Vladimir Berezin, Elisabeth Marianne Bock, Vladislav Kiselyov

18 Citations (Scopus)

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Abstract

The fibroblast growth factor receptor (FGFR) can be activated through direct interaction with the neural cell adhesion molecule (NCAM). The extracellular part of the FGFR consists of three immunoglobulin-like (Ig) modules, and that of the NCAM consists of five Ig and two fibronectin type III (F3) modules. NCAM-FGFR interactions are mediated by the third FGFR Ig module and the second NCAM F3 module. Using surface plasmon resonance and nuclear magnetic resonance analyses, the present study demonstrates that the second Ig module of FGFR also is involved in binding to the NCAM. The second Ig module residues involved in binding were identified and shown to be localized on the "opposite sides" of the module, indicating that when NCAMs are clustered (e.g., due to homophilic binding), high-affinity FGFR binding sites may be formed by the neighboring NCAMs.

Original language	English
Journal	Protein Science
Volume	17
Issue number	10
Pages (from-to)	1698-1705
Number of pages	8
ISSN	0961-8368
DOIs	https://doi.org/10.1110/ps.035964.108
Publication status	Published - 2008

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title = "Structural basis for the activation of FGFR by NCAM",

abstract = "The fibroblast growth factor receptor (FGFR) can be activated through direct interaction with the neural cell adhesion molecule (NCAM). The extracellular part of the FGFR consists of three immunoglobulin-like (Ig) modules, and that of the NCAM consists of five Ig and two fibronectin type III (F3) modules. NCAM-FGFR interactions are mediated by the third FGFR Ig module and the second NCAM F3 module. Using surface plasmon resonance and nuclear magnetic resonance analyses, the present study demonstrates that the second Ig module of FGFR also is involved in binding to the NCAM. The second Ig module residues involved in binding were identified and shown to be localized on the {"}opposite sides{"} of the module, indicating that when NCAMs are clustered (e.g., due to homophilic binding), high-affinity FGFR binding sites may be formed by the neighboring NCAMs.",

author = "Artur Kochoyan and Flemming Poulsen and Vladimir Berezin and Bock, {Elisabeth Marianne} and Vladislav Kiselyov",

note = "Keywords: Animals; Binding Sites; Mice; Models, Molecular; Neural Cell Adhesion Molecules; Protein Binding; Protein Conformation; Protein Interaction Mapping; Rats; Receptors, Fibroblast Growth Factor; Recombinant Proteins",

year = "2008",

doi = "10.1110/ps.035964.108",

language = "English",

volume = "17",

pages = "1698--1705",

journal = "Protein Science",

issn = "0961-8368",

publisher = "Wiley-Blackwell",

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TY - JOUR

T1 - Structural basis for the activation of FGFR by NCAM

AU - Kochoyan, Artur

AU - Poulsen, Flemming

AU - Berezin, Vladimir

AU - Bock, Elisabeth Marianne

AU - Kiselyov, Vladislav

N1 - Keywords: Animals; Binding Sites; Mice; Models, Molecular; Neural Cell Adhesion Molecules; Protein Binding; Protein Conformation; Protein Interaction Mapping; Rats; Receptors, Fibroblast Growth Factor; Recombinant Proteins

PY - 2008

Y1 - 2008

N2 - The fibroblast growth factor receptor (FGFR) can be activated through direct interaction with the neural cell adhesion molecule (NCAM). The extracellular part of the FGFR consists of three immunoglobulin-like (Ig) modules, and that of the NCAM consists of five Ig and two fibronectin type III (F3) modules. NCAM-FGFR interactions are mediated by the third FGFR Ig module and the second NCAM F3 module. Using surface plasmon resonance and nuclear magnetic resonance analyses, the present study demonstrates that the second Ig module of FGFR also is involved in binding to the NCAM. The second Ig module residues involved in binding were identified and shown to be localized on the "opposite sides" of the module, indicating that when NCAMs are clustered (e.g., due to homophilic binding), high-affinity FGFR binding sites may be formed by the neighboring NCAMs.

AB - The fibroblast growth factor receptor (FGFR) can be activated through direct interaction with the neural cell adhesion molecule (NCAM). The extracellular part of the FGFR consists of three immunoglobulin-like (Ig) modules, and that of the NCAM consists of five Ig and two fibronectin type III (F3) modules. NCAM-FGFR interactions are mediated by the third FGFR Ig module and the second NCAM F3 module. Using surface plasmon resonance and nuclear magnetic resonance analyses, the present study demonstrates that the second Ig module of FGFR also is involved in binding to the NCAM. The second Ig module residues involved in binding were identified and shown to be localized on the "opposite sides" of the module, indicating that when NCAMs are clustered (e.g., due to homophilic binding), high-affinity FGFR binding sites may be formed by the neighboring NCAMs.

U2 - 10.1110/ps.035964.108

DO - 10.1110/ps.035964.108

M3 - Journal article

C2 - 18593816

SN - 0961-8368

VL - 17

SP - 1698

EP - 1705

JO - Protein Science

JF - Protein Science

IS - 10

ER -

Structural basis for the activation of FGFR by NCAM

Abstract

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