RGD Reference Report - Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins. - Rat Genome Database

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Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins.

Authors: Lundell, A  Olin, AI  Morgelin, M  Al-Karadaghi, S  Aspberg, A  Logan, DT 
Citation: Lundell A, etal., Structure. 2004 Aug;12(8):1495-506.
RGD ID: 2315856
Pubmed: PMID:15296743   (View Abstract at PubMed)
DOI: DOI:10.1016/j.str.2004.05.021   (Journal Full-text)

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.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
calcium ion binding  IDA 2315856 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Acan  (aggrecan)


Additional Information