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| {{STRUCTURE_2z7x| PDB=2z7x | SCENE= }} | | {{STRUCTURE_2z7x| PDB=2z7x | SCENE= }} |
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| '''Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide'''
| | ===Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide=== |
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| ==Overview==
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| TLR2 in association with TLR1 or TLR6 plays an important role in the innate immune response by recognizing microbial lipoproteins and lipopeptides. Here we present the crystal structures of the human TLR1-TLR2-lipopeptide complex and of the mouse TLR2-lipopeptide complex. Binding of the tri-acylated lipopeptide, Pam(3)CSK(4), induced the formation of an "m" shaped heterodimer of the TLR1 and TLR2 ectodomains whereas binding of the di-acylated lipopeptide, Pam(2)CSK(4), did not. The three lipid chains of Pam(3)CSK(4) mediate the heterodimerization of the receptor; the two ester-bound lipid chains are inserted into a pocket in TLR2, while the amide-bound lipid chain is inserted into a hydrophobic channel in TLR1. An extensive hydrogen-bonding network, as well as hydrophobic interactions, between TLR1 and TLR2 further stabilize the heterodimer. We propose that formation of the TLR1-TLR2 heterodimer brings the intracellular TIR domains close to each other to promote dimerization and initiate signaling.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17889651}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17889651 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17889651}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Tlr2]] | | [[Category: Tlr2]] |
| [[Category: Transmembrane]] | | [[Category: Transmembrane]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 20:01:35 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:22:57 2008'' |