Literature DB >> 30839295

Crystal structure of the legume lectin-like domain of an ERGIC-53-like protein from Entamoeba histolytica.

Farha Khan1, Kaza Suguna1.   

Abstract

ERGIC-53-like proteins are type I membrane proteins that belong to the class of intracellular cargo receptors and are known to be indispensable for the intracellular transport of glycoproteins. They are implicated in transporting glycoproteins between the endoplasmic reticulum and the Golgi body. The crystal structure of the legume lectin-like domain of an ERGIC-53-like protein from Entamoeba histolytica has been determined at 2.4 Å resolution. Although the overall structure of the domain resembles those of its mammalian and yeast orthologs (ERGIC-53 and Emp46, respectively), there are significant changes in the carbohydrate-binding site. A sequence-based search revealed the presence of several homologs of ERGIC-53 in different species of Entamoeba. This is the first report of the structural characterization of a member of this class of proteins from a protozoan and serves to further knowledge and understanding regarding the species-specific differences.

Entities:  

Keywords:  ERGIC-53-like proteins; Entamoeba histolytica; intracellular cargo receptors; legume lectin-like domains; membrane proteins

Mesh:

Substances:

Year:  2019        PMID: 30839295      PMCID: PMC6404861          DOI: 10.1107/S2053230X19000499

Source DB:  PubMed          Journal:  Acta Crystallogr F Struct Biol Commun        ISSN: 2053-230X            Impact factor:   1.056


  63 in total

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Authors:  Yukiko Kamiya; Daiki Kamiya; Kazuo Yamamoto; Beat Nyfeler; Hans-Peter Hauri; Koichi Kato
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9.  Structural basis for recognition of high mannose type glycoproteins by mammalian transport lectin VIP36.

Authors:  Tadashi Satoh; Nathan P Cowieson; Wataru Hakamata; Hiroko Ideo; Keiko Fukushima; Masaaki Kurihara; Ryuichi Kato; Katsuko Yamashita; Soichi Wakatsuki
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  1 in total

Review 1.  A Review: Natural and Synthetic Compounds Targeting Entamoeba histolytica and Its Biological Membrane.

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Journal:  Membranes (Basel)       Date:  2022-04-01
  1 in total

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