1tdq
From Proteopedia
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|PDB= 1tdq |SIZE=350|CAPTION= <scene name='initialview01'>1tdq</scene>, resolution 2.60Å | |PDB= 1tdq |SIZE=350|CAPTION= <scene name='initialview01'>1tdq</scene>, resolution 2.60Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= AGC1, AGC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= AGC1, AGC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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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[[Category: Olin, A I.]] | [[Category: Olin, A I.]] | ||
[[Category: al-Karadaghi, S.]] | [[Category: al-Karadaghi, S.]] | ||
| - | [[Category: CA]] | ||
[[Category: c-type lectin domain]] | [[Category: c-type lectin domain]] | ||
[[Category: extracellular matrix]] | [[Category: extracellular matrix]] | ||
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[[Category: tenascin]] | [[Category: tenascin]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:54:43 2008'' |
Revision as of 20:54, 30 March 2008
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| , resolution 2.60Å | |||||||
|---|---|---|---|---|---|---|---|
| Ligands: | |||||||
| Gene: | AGC1, AGC (Rattus norvegicus) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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