Structural highlights
Publication Abstract from PubMed
The interaction of Trypanosoma brucei (Tb) Pex5p and its receptor TbPex14p is essential for the translocation of newly synthesized matrix proteins into the glycosome. Here, we reveal that only the third WXXXF/Y motif of TbPex5p is involved in the interaction and that negative charge of the fourth amino acid is important. We suggest that Phe35 and Phe52 of TbPex14p interact with Trp318 and Phe322 in the third motif and that the Lys56 adjacent to Phe35/Phe52 associates with the fourth Glu in the motif to make the complex. This information is expected to be useful for developing anti-trypanosomal drugs.
Characterization of the interaction between Trypanosoma brucei Pex5p and its receptor Pex14p.,Watanabe Y, Kawaguchi K, Okuyama N, Sugawara Y, Obita T, Mizuguchi M, Morita M, Imanaka T FEBS Lett. 2015 Dec 21. doi: 10.1002/1873-3468.12044. PMID:26762183[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Watanabe Y, Kawaguchi K, Okuyama N, Sugawara Y, Obita T, Mizuguchi M, Morita M, Imanaka T. Characterization of the interaction between Trypanosoma brucei Pex5p and its receptor Pex14p. FEBS Lett. 2015 Dec 21. doi: 10.1002/1873-3468.12044. PMID:26762183 doi:http://dx.doi.org/10.1002/1873-3468.12044
