1ziw

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(New page: 200px<br /> <applet load="1ziw" size="450" color="white" frame="true" align="right" spinBox="true" caption="1ziw, resolution 2.10&Aring;" /> '''Human Toll-like Rec...)
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[[Image:1ziw.gif|left|200px]]<br />
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[[Image:1ziw.gif|left|200px]]<br /><applet load="1ziw" size="350" color="white" frame="true" align="right" spinBox="true"
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<applet load="1ziw" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1ziw, resolution 2.10&Aring;" />
caption="1ziw, resolution 2.10&Aring;" />
'''Human Toll-like Receptor 3 extracellular domain structure'''<br />
'''Human Toll-like Receptor 3 extracellular domain structure'''<br />
==Overview==
==Overview==
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Toll-like receptors (TLRs) play key roles in activating immune responses, during infection. The human TLR3 ectodomain structure at 2.1 angstroms, reveals a large horseshoe-shaped solenoid assembled from 23 leucine-rich, repeats (LRRs). Asparagines conserved in the 24-residue LRR motif, contribute extensive hydrogen-bonding networks for solenoid stabilization., TLR3 is largely masked by carbohydrate, but one face is, glycosylation-free, which suggests its potential role in ligand binding, and oligomerization. Highly conserved surface residues and a TLR3-specific, LRR insertion form a homodimer interface in the crystal, whereas two, patches of positively charged residues and a second insertion would, provide an appropriate binding site for double-stranded RNA.
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Toll-like receptors (TLRs) play key roles in activating immune responses during infection. The human TLR3 ectodomain structure at 2.1 angstroms reveals a large horseshoe-shaped solenoid assembled from 23 leucine-rich repeats (LRRs). Asparagines conserved in the 24-residue LRR motif contribute extensive hydrogen-bonding networks for solenoid stabilization. TLR3 is largely masked by carbohydrate, but one face is glycosylation-free, which suggests its potential role in ligand binding and oligomerization. Highly conserved surface residues and a TLR3-specific LRR insertion form a homodimer interface in the crystal, whereas two patches of positively charged residues and a second insertion would provide an appropriate binding site for double-stranded RNA.
==About this Structure==
==About this Structure==
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1ZIW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with NDG, NAG, SO4 and GOL as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1ZIW OCA].
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1ZIW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=NDG:'>NDG</scene>, <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=SO4:'>SO4</scene> and <scene name='pdbligand=GOL:'>GOL</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZIW OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Choe, J.]]
[[Category: Choe, J.]]
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[[Category: Wilson, I.A.]]
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[[Category: Wilson, I A.]]
[[Category: GOL]]
[[Category: GOL]]
[[Category: NAG]]
[[Category: NAG]]
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[[Category: innate immunity]]
[[Category: innate immunity]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 20:35:00 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:16:00 2008''

Revision as of 14:16, 21 February 2008


1ziw, resolution 2.10Å

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Human Toll-like Receptor 3 extracellular domain structure

Overview

Toll-like receptors (TLRs) play key roles in activating immune responses during infection. The human TLR3 ectodomain structure at 2.1 angstroms reveals a large horseshoe-shaped solenoid assembled from 23 leucine-rich repeats (LRRs). Asparagines conserved in the 24-residue LRR motif contribute extensive hydrogen-bonding networks for solenoid stabilization. TLR3 is largely masked by carbohydrate, but one face is glycosylation-free, which suggests its potential role in ligand binding and oligomerization. Highly conserved surface residues and a TLR3-specific LRR insertion form a homodimer interface in the crystal, whereas two patches of positively charged residues and a second insertion would provide an appropriate binding site for double-stranded RNA.

About this Structure

1ZIW is a Single protein structure of sequence from Homo sapiens with , , and as ligands. Full crystallographic information is available from OCA.

Reference

Crystal structure of human toll-like receptor 3 (TLR3) ectodomain., Choe J, Kelker MS, Wilson IA, Science. 2005 Jul 22;309(5734):581-5. Epub 2005 Jun 16. PMID:15961631

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