2z66: Difference between revisions
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New page: left|200px<br /> <applet load="2z66" size="450" color="white" frame="true" align="right" spinBox="true" caption="2z66, resolution 1.90Å" /> '''Crystal structure o... |
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[[Image:2z66. | [[Image:2z66.jpg|left|200px]]<br /><applet load="2z66" size="350" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2z66" size=" | |||
caption="2z66, resolution 1.90Å" /> | caption="2z66, resolution 1.90Å" /> | ||
'''Crystal structure of the VT3 hybrid of human TLR4 and hagfish VLRB.61'''<br /> | '''Crystal structure of the VT3 hybrid of human TLR4 and hagfish VLRB.61'''<br /> | ||
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==Overview== | ==Overview== | ||
TLR4 and MD-2 form a heterodimer that recognizes LPS (lipopolysaccharide), from Gram-negative bacteria. Eritoran is an analog of LPS that antagonizes, its activity by binding to the TLR4-MD-2 complex. We determined the, structure of the full-length ectodomain of the mouse TLR4 and MD-2, complex. We also produced a series of hybrids of human TLR4 and hagfish, VLR and determined their structures with and without bound MD-2 and, Eritoran. TLR4 is an atypical member of the LRR family and is composed of, N-terminal, central, and C-terminal domains. The beta sheet of the central, domain shows unusually small radii and large twist angles. MD-2 binds to, the concave surface of the N-terminal and central domains. The interaction, with Eritoran is mediated by a hydrophobic internal pocket in MD-2. Based, on structural analysis and mutagenesis experiments on MD-2 and TLR4, we, propose a model of TLR4-MD-2 dimerization induced by LPS. | TLR4 and MD-2 form a heterodimer that recognizes LPS (lipopolysaccharide), from Gram-negative bacteria. Eritoran is an analog of LPS that antagonizes, its activity by binding to the TLR4-MD-2 complex. We determined the, structure of the full-length ectodomain of the mouse TLR4 and MD-2, complex. We also produced a series of hybrids of human TLR4 and hagfish, VLR and determined their structures with and without bound MD-2 and, Eritoran. TLR4 is an atypical member of the LRR family and is composed of, N-terminal, central, and C-terminal domains. The beta sheet of the central, domain shows unusually small radii and large twist angles. MD-2 binds to, the concave surface of the N-terminal and central domains. The interaction, with Eritoran is mediated by a hydrophobic internal pocket in MD-2. Based, on structural analysis and mutagenesis experiments on MD-2 and TLR4, we, propose a model of TLR4-MD-2 dimerization induced by LPS. | ||
==About this Structure== | ==About this Structure== | ||
2Z66 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eptatretus_burgeri,_homo_sapiens Eptatretus burgeri, homo sapiens] with SO4 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | 2Z66 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Eptatretus_burgeri,_homo_sapiens Eptatretus burgeri, homo sapiens] with <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2Z66 OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: transmembrane]] | [[Category: transmembrane]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jan 23 13:36:33 2008'' | ||
