1TDQ

Structural basis for the interactions between tenascins and the C-type lectin domains from lecticans: evidence for a cross-linking role for tenascins

Summary for 1TDQ

• Entry DOI: 10.2210/pdb1tdq/pdb
• Descriptor: Tenascin-R, Aggrecan core protein, CALCIUM ION, ... (4 entities in total)
• Functional Keywords: extracellular matrix, lecticans, tenascins, protein-protein interactions, c-type lectin domain
• Biological source: Rattus norvegicus (Norway rat); More
• Cellular location: Secreted, extracellular space, extracellular matrix: Q05546 P07897
• Total number of polymer chains: 2
• Total formula weight: 46125.98

Authors

Lundell, A.,Olin, A.I.,Moergelin, M.,al-Karadaghi, S.,Aspberg, A.,Logan, D.T. (deposition date: 2004-05-24, release date: 2004-08-31, Last modification date: 2024-10-30)

Primary citation

Lundell, A.,Olin, A.I.,Moergelin, M.,al-Karadaghi, S.,Aspberg, A.,Logan, D.T.
Structural basis for interactions between tenascins and lectican C-type lectin domains: evidence for a crosslinking role for tenascins
Structure, 12:1495-1506, 2004

PubMed 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.

PubMed: 15296743
DOI: 10.1016/j.str.2004.05.021

Experimental method

X-RAY DIFFRACTION (2.6 Å)