Advanced

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:
author
organization
publishing date
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
2007-07-05 08:28:33
date last changed
2017-11-05 03:32:44
@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},
  volume       = {12},
  year         = {2004},
}