2z66
From Proteopedia
(New page: 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. | ||
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| - | ==Disease== | ||
| - | Known diseases associated with this structure: Colorectal cancer, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603030 603030]], Endotoxin hyporesponsiveness OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603030 603030]], Longevity, susceptibility to OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603030 603030]], Macular degeneration, age-related, 10 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=603030 603030]] | ||
==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'' |
Revision as of 11:36, 23 January 2008
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Crystal structure of the VT3 hybrid of human TLR4 and hagfish VLRB.61
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.
About this Structure
2Z66 is a Single protein structure of sequence from Eptatretus burgeri, homo sapiens with as ligand. Full crystallographic information is available from OCA.
Reference
Crystal Structure of the TLR4-MD-2 Complex with Bound Endotoxin Antagonist Eritoran., Kim HM, Park BS, Kim JI, Kim SE, Lee J, Oh SC, Enkhbayar P, Matsushima N, Lee H, Yoo OJ, Lee JO, Cell. 2007 Sep 7;130(5):906-17. PMID:17803912
Page seeded by OCA on Wed Jan 23 13:36:33 2008
Categories: Eptatretus burgeri, homo sapiens | Single protein | Kim, H.M. | Lee, J.O. | Park, B.S. | SO4 | Glycoprotein | Immune response | Immune system | Inflammatory response | Innate immunity | Leucine-rich repeat | Lps | Md-2 | Membrane | Polymorphism | Tlr4 | Toll-like receptor | Transmembrane
