2z80: Difference between revisions

Revision as of 19:15, 27 July 2008

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File:2z80.png

Template:STRUCTURE 2z80

Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptideCrystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide

Template:ABSTRACT PUBMED 17889651

About this StructureAbout this Structure

2Z80 is a Single protein structure of sequence from Homo sapiens, eptatretus burgeri. Full crystallographic information is available from OCA.

ReferenceReference

Crystal structure of the TLR1-TLR2 heterodimer induced by binding of a tri-acylated lipopeptide., Jin MS, Kim SE, Heo JY, Lee ME, Kim HM, Paik SG, Lee H, Lee JO, Cell. 2007 Sep 21;130(6):1071-82. PMID:17889651

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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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===
-==Overview==
+<!--
-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}}
 ==About this Structure==
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 [[Category: Tlr2]]
 [[Category: Transmembrane]]
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