Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins.
Lundell, Anna ; Olin, Anders LU ; Mörgelin, Matthias LU ; Al-Karadaghi, Salam LU ; Aspberg, Anders LU
and Logan, Derek
LU
(2004)
In Structure
12(8).
p.1495-1506
- Abstract
- The C-terminal G3 domains of lecticans mediate crosslinking to diverse extracellular matrix (ECM) proteins during ECM assembly, through their C-type lectin (CLD) subdomains. The structure of the rat aggrecan CLD in a Ca(2+)-dependent complex with fibronectin type III repeats 3-5 of rat tenascin-R provides detailed support for such crosslinking. The CLD loops bind Ca2+ like other CLDs, but no carbohydrate binding is observed or possible. This is thus the first example of a direct Ca(2+)-dependent protein-protein interaction of a CLD. Surprisingly, tenascin-R does not coordinate the Ca2+ ions directly. Electron microscopy confirms that full-length tenascin-R and tenascin-C crosslink hyaluronan-aggrecan complexes. The results are significant... (More)
- The C-terminal G3 domains of lecticans mediate crosslinking to diverse extracellular matrix (ECM) proteins during ECM assembly, through their C-type lectin (CLD) subdomains. The structure of the rat aggrecan CLD in a Ca(2+)-dependent complex with fibronectin type III repeats 3-5 of rat tenascin-R provides detailed support for such crosslinking. The CLD loops bind Ca2+ like other CLDs, but no carbohydrate binding is observed or possible. This is thus the first example of a direct Ca(2+)-dependent protein-protein interaction of a CLD. Surprisingly, tenascin-R does not coordinate the Ca2+ ions directly. Electron microscopy confirms that full-length tenascin-R and tenascin-C crosslink hyaluronan-aggrecan complexes. The results are significant for the binding of all lectican CLDs to tenascin-R and tenascin-C. Comparison of the protein interaction surface with that of P-selectin in complex with the PGSL-1 peptide suggests that direct protein-protein interactions of Ca(2+)-binding CLDs may be more widespread than previously appreciated. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/126816
- author
- Lundell, Anna
; Olin, Anders
LU
; Mörgelin, Matthias
LU
; Al-Karadaghi, Salam
LU
; Aspberg, Anders
LU
and Logan, Derek
LU
- organization
- publishing date
- 2004
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Structure
- volume
- 12
- issue
- 8
- pages
- 1495 - 1506
- publisher
- Cell Press
- external identifiers
-
- pmid:15296743
- wos:000223394200020
- scopus:4143100146
- ISSN
- 0969-2126
- DOI
- 10.1016/j.str.2004.05.021
- language
- English
- LU publication?
- yes
- id
- fc44b6b2-f4bc-4050-8906-e636f7a2743a (old id 126816)
- alternative location
- http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=Retrieve&db=PubMed&list_uids=15296743&dopt=Abstract
- date added to LUP
- 2016-04-01 11:48:41
- date last changed
- 2022-04-20 22:08:58
@article{fc44b6b2-f4bc-4050-8906-e636f7a2743a,
abstract = {{The C-terminal G3 domains of lecticans mediate crosslinking to diverse extracellular matrix (ECM) proteins during ECM assembly, through their C-type lectin (CLD) subdomains. The structure of the rat aggrecan CLD in a Ca(2+)-dependent complex with fibronectin type III repeats 3-5 of rat tenascin-R provides detailed support for such crosslinking. The CLD loops bind Ca2+ like other CLDs, but no carbohydrate binding is observed or possible. This is thus the first example of a direct Ca(2+)-dependent protein-protein interaction of a CLD. Surprisingly, tenascin-R does not coordinate the Ca2+ ions directly. Electron microscopy confirms that full-length tenascin-R and tenascin-C crosslink hyaluronan-aggrecan complexes. The results are significant for the binding of all lectican CLDs to tenascin-R and tenascin-C. Comparison of the protein interaction surface with that of P-selectin in complex with the PGSL-1 peptide suggests that direct protein-protein interactions of Ca(2+)-binding CLDs may be more widespread than previously appreciated.}},
author = {{Lundell, Anna and Olin, Anders and Mörgelin, Matthias and Al-Karadaghi, Salam and Aspberg, Anders and Logan, Derek}},
issn = {{0969-2126}},
language = {{eng}},
number = {{8}},
pages = {{1495--1506}},
publisher = {{Cell Press}},
series = {{Structure}},
title = {{Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins.}},
url = {{http://dx.doi.org/10.1016/j.str.2004.05.021}},
doi = {{10.1016/j.str.2004.05.021}},
volume = {{12}},
year = {{2004}},
}