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1tdq

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[[Image:1tdq.gif|left|200px]]
[[Image:1tdq.gif|left|200px]]
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{{Structure
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|GENE= AGC1, AGC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1tdq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1tdq OCA], [http://www.ebi.ac.uk/pdbsum/1tdq PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1tdq RCSB]</span>
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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.]]
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[[Category: al-Karadaghi, S.]]
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[[Category: Al-Karadaghi, S.]]
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[[Category: c-type lectin domain]]
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[[Category: C-type lectin domain]]
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[[Category: extracellular matrix]]
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[[Category: Extracellular matrix]]
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[[Category: lectican]]
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[[Category: Lectican]]
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[[Category: protein-protein interaction]]
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[[Category: Protein-protein interaction]]
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[[Category: tenascin]]
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[[Category: Tenascin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 09:49:51 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:54:43 2008''
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Revision as of 06:49, 3 May 2008

Template:STRUCTURE 1tdq

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

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