Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the N-terminal carbohydrate-recognition domain of human galectin-4.

Abstract

Galectin-4 is a tandem-repeat-type galectin that is expressed in the epithelium of the alimentary tract from the tongue to the large intestine. Additionally, strong expression of galectin-4 can also be induced in cancers in other tissues, including the breast and liver. In order to explore its potential as a target for anticancer drug design, elucidation of the structural basis of the carbohydrate-binding specificities of galectin-4 has been focused on. As an initial step, the N-terminal carbohydrate-recognition domain of human galectin-4 (hGal4-CRD-1) has been successfully crystallized using the vapour-diffusion technique, a complete data set has been collected to 2.2 A resolution and the structure has been solved by the molecular-replacement technique. The crystals belonged to space group P6(1)22, with unit-cell parameters a = b = 71.25, c = 108.66 A. The asymmetric unit contained one molecule of hGal4-CRD-1, with a V(M) value of 2.34 A(3) Da(-1) and a solvent content of 47.51%.

• Authors: Ana Lucia L R Zimbardi, Matheus P Pinheiro, Marcelo Dias-Baruffi, M Cristina Nonato
• Journal: Acta crystallographica. Section F, Structural biology and crystallization communications (Acta Crystallogr Sect F Struct Biol Cryst Commun) Vol. 66 Issue Pt 5 Pg. 542-5 (May 01 2010) ISSN: 1744-3091 [Electronic] England
• PMID: 20445255 (Publication Type: Journal Article, Research Support, Non-U.S. Gov't)

Chemical References

• Carbohydrates
• Galectin 4

Topics

• Carbohydrates (chemistry)
• Cloning, Molecular
• Crystallography, X-Ray
• Galectin 4 (chemistry, isolation & purification)
• Humans