The laminin-binding domain of agrin is structurally related to N-TIMP-1

Richard Kammerer; Jörg Stetefeld; Margrit Jenny; Therese Schulthess; Ruth Landwehr; Beat Schumacher; Sabine Frank; Markus A. Rüegg; Jürgen Engel; Richard A. Kammerer

doi:10.1038/90422

The laminin-binding domain of agrin is structurally related to N-TIMP-1

Richard Kammerer, Jörg Stetefeld, Margrit Jenny, Therese Schulthess, Ruth Landwehr, Beat Schumacher, Sabine Frank, Markus A. Rüegg, Jürgen Engel, Richard A. Kammerer

Research output: Contribution to journal › Article › peer-review

Abstract

Agrin is the key organizer of postsynaptic differentiation at the neuromuscular junction. This organization activity requires the binding of agrin to the synaptic basal lamina. Binding is conferred by the N-terminal agrin (NtA) domain, which mediates a high-affinity interaction with the coiled coil domain of laminins. Here, we report the crystal structure of chicken NtA at 1.6 Å resolution. The structure reveals that NtA harbors an oligosaccharide/oligonucleotide-binding fold with several possible sites for the interaction with different ligands. A high structural similarity of NtA with the protease inhibition domain in tissue inhibitor of metalloproteinases-1 (TIMP-1) supports the idea of additional functions of agrin besides synaptogenic activity.

Original language	English
Pages (from-to)	705-709
Number of pages	4
Journal	Nature Structural Biology
Volume	8
Issue number	8
DOIs	https://doi.org/10.1038/90422
Publication status	Published - 2001

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title = "The laminin-binding domain of agrin is structurally related to N-TIMP-1",

abstract = "Agrin is the key organizer of postsynaptic differentiation at the neuromuscular junction. This organization activity requires the binding of agrin to the synaptic basal lamina. Binding is conferred by the N-terminal agrin (NtA) domain, which mediates a high-affinity interaction with the coiled coil domain of laminins. Here, we report the crystal structure of chicken NtA at 1.6 {\AA} resolution. The structure reveals that NtA harbors an oligosaccharide/oligonucleotide-binding fold with several possible sites for the interaction with different ligands. A high structural similarity of NtA with the protease inhibition domain in tissue inhibitor of metalloproteinases-1 (TIMP-1) supports the idea of additional functions of agrin besides synaptogenic activity.",

author = "Richard Kammerer and J{\"o}rg Stetefeld and Margrit Jenny and Therese Schulthess and Ruth Landwehr and Beat Schumacher and Sabine Frank and R{\"u}egg, {Markus A.} and J{\"u}rgen Engel and Kammerer, {Richard A.}",

year = "2001",

doi = "10.1038/90422",

language = "English",

volume = "8",

pages = "705--709",

journal = "Nature Structural Biology",

publisher = "Springer Nature",

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TY - JOUR

T1 - The laminin-binding domain of agrin is structurally related to N-TIMP-1

AU - Kammerer, Richard

AU - Stetefeld, Jörg

AU - Jenny, Margrit

AU - Schulthess, Therese

AU - Landwehr, Ruth

AU - Schumacher, Beat

AU - Frank, Sabine

AU - Rüegg, Markus A.

AU - Engel, Jürgen

AU - Kammerer, Richard A.

PY - 2001

Y1 - 2001

N2 - Agrin is the key organizer of postsynaptic differentiation at the neuromuscular junction. This organization activity requires the binding of agrin to the synaptic basal lamina. Binding is conferred by the N-terminal agrin (NtA) domain, which mediates a high-affinity interaction with the coiled coil domain of laminins. Here, we report the crystal structure of chicken NtA at 1.6 Å resolution. The structure reveals that NtA harbors an oligosaccharide/oligonucleotide-binding fold with several possible sites for the interaction with different ligands. A high structural similarity of NtA with the protease inhibition domain in tissue inhibitor of metalloproteinases-1 (TIMP-1) supports the idea of additional functions of agrin besides synaptogenic activity.

AB - Agrin is the key organizer of postsynaptic differentiation at the neuromuscular junction. This organization activity requires the binding of agrin to the synaptic basal lamina. Binding is conferred by the N-terminal agrin (NtA) domain, which mediates a high-affinity interaction with the coiled coil domain of laminins. Here, we report the crystal structure of chicken NtA at 1.6 Å resolution. The structure reveals that NtA harbors an oligosaccharide/oligonucleotide-binding fold with several possible sites for the interaction with different ligands. A high structural similarity of NtA with the protease inhibition domain in tissue inhibitor of metalloproteinases-1 (TIMP-1) supports the idea of additional functions of agrin besides synaptogenic activity.

U2 - 10.1038/90422

DO - 10.1038/90422

M3 - Article

C2 - 11473262

VL - 8

SP - 705

EP - 709

JO - Nature Structural Biology

JF - Nature Structural Biology

IS - 8

ER -

The laminin-binding domain of agrin is structurally related to N-TIMP-1

Abstract

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