1tdq: Difference between revisions
New page: left|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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[[Image:1tdq.gif|left|200px]]<br /><applet load="1tdq" size=" | [[Image:1tdq.gif|left|200px]]<br /><applet load="1tdq" size="350" color="white" frame="true" align="right" spinBox="true" | ||
caption="1tdq, resolution 2.60Å" /> | caption="1tdq, resolution 2.60Å" /> | ||
'''Structural basis for the interactions between tenascins and the C-type lectin domains from lecticans: evidence for a cross-linking role for tenascins'''<br /> | '''Structural basis for the interactions between tenascins and the C-type lectin domains from lecticans: evidence for a cross-linking role for tenascins'''<br /> | ||
==Overview== | ==Overview== | ||
The C-terminal G3 domains of lecticans mediate crosslinking to diverse | 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== | ==About this Structure== | ||
1TDQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 1TDQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TDQ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Aspberg, A.]] | [[Category: Aspberg, A.]] | ||
[[Category: Logan, D | [[Category: Logan, D T.]] | ||
[[Category: Lundell, A.]] | [[Category: Lundell, A.]] | ||
[[Category: Moergelin, M.]] | [[Category: Moergelin, M.]] | ||
[[Category: Olin, A | [[Category: Olin, A I.]] | ||
[[Category: al-Karadaghi, S.]] | [[Category: al-Karadaghi, S.]] | ||
[[Category: CA]] | [[Category: CA]] | ||
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[[Category: tenascins]] | [[Category: tenascins]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:30 2008'' | ||
Revision as of 13:12, 21 February 2008
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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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