Structural basis of the collagen-binding mode of discoidin domain receptor 2

Osamu Ichikawa; Masanori Osawa; Noritaka Nishida; Naoki Goshima; Nobuo Nomura; Ichio Shimada

doi:10.1038/sj.emboj.7601833

Structural basis of the collagen-binding mode of discoidin domain receptor 2

Osamu Ichikawa, Masanori Osawa, Noritaka Nishida, Naoki Goshima, Nobuo Nomura, Ichio Shimada

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

86 Citations (Scopus)

Abstract

Discoidin domain receptor (DDR) is a cell-surface receptor tyrosine kinase activated by the binding of its discoidin (DS) domain to fibrillar collagen. Here, we have determined the NMR structure of the DS domain in DDR2 (DDR2-DS domain), and identified the binding site to fibrillar collagen by transferred cross-saturation experiments. The DDR2-DS domain structure adopts a distorted jellyroll fold, consisting of eight β-strands. The collagen-binding site is formed at the interloop trench, consisting of charged residues surrounded by hydrophobic residues. The surface profile of the collagen-binding site suggests that the DDR2-DS domain recognizes specific sites on fibrillar collagen. This study provides a molecular basis for the collagen-binding mode of the DDR2-DS domain.

Original language	English
Pages (from-to)	4168-4176
Number of pages	9
Journal	EMBO Journal
Volume	26
Issue number	18
DOIs	https://doi.org/10.1038/sj.emboj.7601833
Publication status	Published - 2007 Sep 19
Externally published	Yes

Keywords

Collagen
Discoidin domain receptor
NMR
Protein-protein interaction
Transferred cross-saturation

ASJC Scopus subject areas

Neuroscience(all)
Molecular Biology
Biochemistry, Genetics and Molecular Biology(all)
Immunology and Microbiology(all)

Access to Document

10.1038/sj.emboj.7601833

Fingerprint Dive into the research topics of 'Structural basis of the collagen-binding mode of discoidin domain receptor 2'. Together they form a unique fingerprint.

Cite this

@article{6ae4e2c06f524ca0a2f9431c1995b24d,

title = "Structural basis of the collagen-binding mode of discoidin domain receptor 2",

abstract = "Discoidin domain receptor (DDR) is a cell-surface receptor tyrosine kinase activated by the binding of its discoidin (DS) domain to fibrillar collagen. Here, we have determined the NMR structure of the DS domain in DDR2 (DDR2-DS domain), and identified the binding site to fibrillar collagen by transferred cross-saturation experiments. The DDR2-DS domain structure adopts a distorted jellyroll fold, consisting of eight β-strands. The collagen-binding site is formed at the interloop trench, consisting of charged residues surrounded by hydrophobic residues. The surface profile of the collagen-binding site suggests that the DDR2-DS domain recognizes specific sites on fibrillar collagen. This study provides a molecular basis for the collagen-binding mode of the DDR2-DS domain.",

keywords = "Collagen, Discoidin domain receptor, NMR, Protein-protein interaction, Transferred cross-saturation",

author = "Osamu Ichikawa and Masanori Osawa and Noritaka Nishida and Naoki Goshima and Nobuo Nomura and Ichio Shimada",

year = "2007",

month = sep,

day = "19",

doi = "10.1038/sj.emboj.7601833",

language = "English",

volume = "26",

pages = "4168--4176",

journal = "EMBO Journal",

issn = "0261-4189",

publisher = "Nature Publishing Group",

number = "18",

}

TY - JOUR

T1 - Structural basis of the collagen-binding mode of discoidin domain receptor 2

AU - Ichikawa, Osamu

AU - Osawa, Masanori

AU - Nishida, Noritaka

AU - Goshima, Naoki

AU - Nomura, Nobuo

AU - Shimada, Ichio

PY - 2007/9/19

Y1 - 2007/9/19

N2 - Discoidin domain receptor (DDR) is a cell-surface receptor tyrosine kinase activated by the binding of its discoidin (DS) domain to fibrillar collagen. Here, we have determined the NMR structure of the DS domain in DDR2 (DDR2-DS domain), and identified the binding site to fibrillar collagen by transferred cross-saturation experiments. The DDR2-DS domain structure adopts a distorted jellyroll fold, consisting of eight β-strands. The collagen-binding site is formed at the interloop trench, consisting of charged residues surrounded by hydrophobic residues. The surface profile of the collagen-binding site suggests that the DDR2-DS domain recognizes specific sites on fibrillar collagen. This study provides a molecular basis for the collagen-binding mode of the DDR2-DS domain.

AB - Discoidin domain receptor (DDR) is a cell-surface receptor tyrosine kinase activated by the binding of its discoidin (DS) domain to fibrillar collagen. Here, we have determined the NMR structure of the DS domain in DDR2 (DDR2-DS domain), and identified the binding site to fibrillar collagen by transferred cross-saturation experiments. The DDR2-DS domain structure adopts a distorted jellyroll fold, consisting of eight β-strands. The collagen-binding site is formed at the interloop trench, consisting of charged residues surrounded by hydrophobic residues. The surface profile of the collagen-binding site suggests that the DDR2-DS domain recognizes specific sites on fibrillar collagen. This study provides a molecular basis for the collagen-binding mode of the DDR2-DS domain.

KW - Collagen

KW - Discoidin domain receptor

KW - NMR

KW - Protein-protein interaction

KW - Transferred cross-saturation

UR - http://www.scopus.com/inward/record.url?scp=34648819975&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34648819975&partnerID=8YFLogxK

U2 - 10.1038/sj.emboj.7601833

DO - 10.1038/sj.emboj.7601833

M3 - Article

C2 - 17703188

AN - SCOPUS:34648819975

VL - 26

SP - 4168

EP - 4176

JO - EMBO Journal

JF - EMBO Journal

SN - 0261-4189

IS - 18

ER -

Structural basis of the collagen-binding mode of discoidin domain receptor 2

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Cite this