1tdq
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(New page: 200px<br /><applet load="1tdq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1tdq, resolution 2.60Å" /> '''Structural basis for...)
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Revision as of 01:04, 21 November 2007
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Structural basis for the interactions between tenascins and the C-type lectin domains from lecticans: evidence for a cross-linking role for tenascins
Overview
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.
About this Structure
1TDQ is a Protein complex structure of sequences from Rattus norvegicus with CA as ligand. Full crystallographic information is available from OCA.
Reference
Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins., Lundell A, Olin AI, Morgelin M, al-Karadaghi S, Aspberg A, Logan DT, Structure. 2004 Aug;12(8):1495-506. PMID:15296743
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