Abstract：
:The structure of full-length human TLR5 determined by electron microscopy single-particle image reconstruction at 26Å resolution shows that TLR5 forms an asymmetric homodimer via ectodomain interactions. The structure shows that like TLR9, TLR5 dimerizes in the absence of ligand. The asymmetry of the dimer suggests that TLR5 may recognize two flagellin molecules cooperatively to establish an optimal flagellin response threshold. A TLR5 homology model was generated and fitted into the electron microscopy structure. All seven predicted N-linked glycosylation sites are exposed on the molecular surface, away from the dimer interface. Glycosylation at the first five sites was confirmed by tandem mass spectrometry. Two aspartate residues proposed to interact with flagellin (Asp294 and Asp366) are sterically occluded by a glycan at position 342. In contrast, the central region of the ectodomains near the dimer interface is unobstructed by glycans. Ligand binding in this region would be consistent with the ligand binding sites of other TLRs.
journal_name
J Struct Bioljournal_title
Journal of structural biologyauthors
Zhou K,Kanai R,Lee P,Wang HW,Modis Ydoi
10.1016/j.jsb.2011.12.002subject
Has Abstractpub_date
2012-02-01 00:00:00pages
402-9issue
2eissn
1047-8477issn
1095-8657pii
S1047-8477(11)00348-0journal_volume
177pub_type
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journal_title：Journal of structural biology
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journal_title：Journal of structural biology
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journal_title：Journal of structural biology
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pub_type： 杂志文章,评审
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