Full-length model of the human galectin-4 and insights into dynamics of inter-domain communication

Joane K. Rustiguel, Ricardo O.S. Soares, Steve P. Meisburger, Katherine M. Davis, Kristina L. Malzbender, Nozomi Ando, Marcelo Dias-Baruffi, Maria Cristina Nonato

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4 Scopus citations

Abstract

Galectins are proteins involved in diverse cellular contexts due to their capacity to decipher and respond to the information encoded by β-galactoside sugars. In particular, human galectin-4, normally expressed in the healthy gastrointestinal tract, displays differential expression in cancerous tissues and is considered a potential drug target for liver and lung cancer. Galectin-4 is a tandem-repeat galectin characterized by two carbohydrate recognition domains connected by a linker-peptide. Despite their relevance to cell function and pathogenesis, structural characterization of full-length tandem-repeat galectins has remained elusive. Here, we investigate galectin-4 using X-ray crystallography, small-and wide-Angle X-ray scattering, molecular modelling, molecular dynamics simulations, and differential scanning fluorimetry assays and describe for the first time a structural model for human galectin-4. Our results provide insight into the structural role of the linker-peptide and shed light on the dynamic characteristics of the mechanism of carbohydrate recognition among tandem-repeat galectins.

Original languageEnglish (US)
Article number33633
JournalScientific reports
Volume6
DOIs
StatePublished - Sep 19 2016

All Science Journal Classification (ASJC) codes

  • General

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    Rustiguel, J. K., Soares, R. O. S., Meisburger, S. P., Davis, K. M., Malzbender, K. L., Ando, N., Dias-Baruffi, M., & Nonato, M. C. (2016). Full-length model of the human galectin-4 and insights into dynamics of inter-domain communication. Scientific reports, 6, [33633]. https://doi.org/10.1038/srep33633