title: Solution structure of Q388A3 PDZ domain from Trypanosoma brucei.
abstract: PDZ domains are abundant protein interaction modules that often recognize short amino acid motifs at the C-termini of target proteins and regulate multiple biological processes. So far, no PDZ domain in Trypanosoma brucei, an eukaryotic parasite causing sleeping sickness, has been studied. Q388A3, conserved in the related kinetoplastid parasites, is a 1634-residue protein containing a PDZ domain at its C-terminus. In this work, the solution structure of Q388A3 PDZ domain was solved by NMR spectroscopy. Q388A3 PDZ domain adopts a PDZ-like fold composed by a five-stranded β-sheet capped by two α-helices, which is similar to the PDZ domains from HtrA family proteins. Meanwhile, Q388A3 PDZ domain shows some structural features quite different from HtrA PDZ domain.
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
authors.forename: Song
authors.initials: S
authors.lastname: Mei
authors.affiliation: School of Life Sciences, Anhui University, Hefei, Anhui 230039, PR China.
authors.forename: Yuanqiu
authors.initials: Y
authors.lastname: Dong
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China.
authors.forename: Jiahai
authors.initials: J
authors.lastname: Zhang
authors.affiliation: School of Life Sciences, Anhui University, Hefei, Anhui 230039, PR China.
authors.forename: Xuecheng
authors.initials: X
authors.lastname: Zhang
authors.affiliation: Hefei National Laboratory for Physical Sciences at Microscale, School of Life Sciences, University of Science and Technology of China, Hefei, Anhui 230026, PR China. Electronic address: xmtu@ustc.edu.cn.
authors.forename: Xiaoming
authors.initials: X
authors.lastname: Tu
mesh_terms: D000595:Amino Acid Sequence; D001665:Binding Sites; D003001:Cloning, Molecular; D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism; D015870:Gene Expression; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D009682:Magnetic Resonance Spectroscopy; D008958:Models, Molecular; D054731:PDZ Domains; D033903:Periplasmic Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D011485:Protein Binding; D000072417:Protein Domains; D017510:Protein Folding; D017433:Protein Structure, Secondary; D015800:Protozoan Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D016415:Sequence Alignment; D017386:Sequence Homology, Amino Acid; D012697:Serine Endopeptidases / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D014346:Trypanosoma brucei brucei / Q000737:chemistry* / Q000378:metabolism
chemical_list: D006360:Heat-Shock Proteins; D033903:Periplasmic Proteins; D015800:Protozoan Proteins; D011994:Recombinant Proteins; C061682:DegP protease; D012697:Serine Endopeptidases
keywords: NMR; PDZ domain; Trypanosoma brucei