1tdq

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1tdq.gif|left|200px]]<br /><applet load="1tdq" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1tdq.gif|left|200px]]
-
caption="1tdq, resolution 2.60&Aring;" />
+
 
-
'''Structural basis for the interactions between tenascins and the C-type lectin domains from lecticans: evidence for a cross-linking role for tenascins'''<br />
+
{{Structure
 +
|PDB= 1tdq |SIZE=350|CAPTION= <scene name='initialview01'>1tdq</scene>, resolution 2.60&Aring;
 +
|SITE=
 +
|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
 +
|ACTIVITY=
 +
|GENE= AGC1, AGC ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
 +
}}
 +
 
 +
'''Structural basis for the interactions between tenascins and the C-type lectin domains from lecticans: evidence for a cross-linking role for tenascins'''
 +
 
==Overview==
==Overview==
Line 7: Line 16:
==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 <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].
+
1TDQ is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1TDQ OCA].
==Reference==
==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:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=15296743 15296743]
+
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:[http://www.ncbi.nlm.nih.gov/pubmed/15296743 15296743]
[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
Line 22: Line 31:
[[Category: c-type lectin domain]]
[[Category: c-type lectin domain]]
[[Category: extracellular matrix]]
[[Category: extracellular matrix]]
-
[[Category: lecticans]]
+
[[Category: lectican]]
-
[[Category: protein-protein interactions]]
+
[[Category: protein-protein interaction]]
-
[[Category: tenascins]]
+
[[Category: tenascin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:12:30 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 14:17:02 2008''

Revision as of 12:17, 20 March 2008


PDB ID 1tdq

Drag the structure with the mouse to rotate
, resolution 2.60Å
Ligands:
Gene: AGC1, AGC (Rattus norvegicus)
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

Page seeded by OCA on Thu Mar 20 14:17:02 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools