Crystal structure of peptidoglycan recognition protein LB from Drosophila melanogaster

Cited 181 time in webofscience Cited 177 time in scopus
  • Hit : 428
  • Download : 0
The family of peptidoglycan recognition proteins (PGRPs) are associated with the recognition of the peptidoglycan of microbes and subsequent activation of signaling pathways for immune response. Here the crystal structure of Drosophila PGRP-LB is determined at a resolution of 2.0 Angstrom and shows an active-site cleft with a zinc cage. Poor conservation of surface residues at the cleft predicts a widely varying individual specificity of PGRPs for molecular patterns on microbial cell walls. At the back of this cleft is a putatively conserved distinctive groove. The location and mainly hydrophobic nature of the groove indicate that the back face serves for subsequent signaling after clustering of PGRP molecules by binding to polymeric cell wall components.
Publisher
NATURE PUBLISHING GROUP
Issue Date
2003-08
Language
English
Article Type
Article
Keywords

POSITIVE BACTERIAL-INFECTIONS; IMMUNE-RESPONSE REQUIRES; GRAM-NEGATIVE BACTERIA; KAPPA-B KINASE; INNATE IMMUNITY; ANTIBACTERIAL DEFENSE; HOST-DEFENSE; BOMBYX-MORI; TOLL; SYSTEM

Citation

NATURE IMMUNOLOGY, v.4, no.8, pp.787 - 793

ISSN
1529-2908
DOI
10.1038/ni952
URI
http://hdl.handle.net/10203/85639
Appears in Collection
BS-Journal Papers(저널논문)
Files in This Item
There are no files associated with this item.
This item is cited by other documents in WoS
⊙ Detail Information in WoSⓡ Click to see webofscience_button
⊙ Cited 181 items in WoS Click to see citing articles in records_button

qr_code

  • mendeley

    citeulike


rss_1.0 rss_2.0 atom_1.0