1tdq
From Proteopedia
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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''' | '''Structural basis for the interactions between tenascins and the C-type lectin domains from lecticans: evidence for a cross-linking role for tenascins''' | ||
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[[Category: Moergelin, M.]] | [[Category: Moergelin, M.]] | ||
[[Category: Olin, A I.]] | [[Category: Olin, A I.]] | ||
| - | [[Category: | + | [[Category: Al-Karadaghi, S.]] |
| - | [[Category: | + | [[Category: C-type lectin domain]] |
| - | [[Category: | + | [[Category: Extracellular matrix]] |
| - | [[Category: | + | [[Category: Lectican]] |
| - | [[Category: | + | [[Category: Protein-protein interaction]] |
| - | [[Category: | + | [[Category: Tenascin]] |
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| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 06:49, 3 May 2008
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. 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 Page seeded by OCA on Sat May 3 09:49:51 2008
