1tdq: Difference between revisions

From Proteopedia
Jump to navigationJump to search
← Older editNewer edit →
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
OCA (talk | contribs)
Bots, Bureaucrats, journal, Administrators
3,332,843 edits
No edit summary
Line 1: Line 1:
[[Image:1tdq.gif|left|200px]]
{{Seed}}
[[Image:1tdq.png|left|200px]]


<!--
<!--
Line 9: Line 10:
{{STRUCTURE_1tdq|  PDB=1tdq  |  SCENE=  }}  
{{STRUCTURE_1tdq|  PDB=1tdq  |  SCENE=  }}  


'''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===




==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.
The line below this paragraph, {{ABSTRACT_PUBMED_15296743}}, adds the Publication Abstract to the page
(as it appears on PubMed at http://www.pubmed.gov), where 15296743 is the PubMed ID number.
-->
{{ABSTRACT_PUBMED_15296743}}


==About this Structure==
==About this Structure==
Line 33: Line 37:
[[Category: Protein-protein interaction]]
[[Category: Protein-protein interaction]]
[[Category: Tenascin]]
[[Category: Tenascin]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 09:49:51 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 15:50:54 2008''

Revision as of 12:51, 29 July 2008

File:1tdq.png

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

Template:ABSTRACT PUBMED 15296743

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 Tue Jul 29 15:50:54 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "https://proteopedia.org/index.php?title=1tdq&oldid=747814"