Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the N-terminal carbohydrate-recognition domain of human galectin-4.
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%.
Zimbardi
Ana Lucia L R
AL
Laboratório de Cristalografia de Proteínas, Departamento de Física e Química, Faculdade de Ciências Farmacêuticas de Ribeirão Preto - USP, Ribeirão Preto - SP, 14040-903, Brazil.
Pinheiro
Matheus P
MP
Dias-Baruffi
Marcelo
M
Nonato
M Cristina
MC
D002241:Carbohydrates / Q000737:chemistry*; D003001:Cloning, Molecular; D018360:Crystallography, X-Ray; D037541:Galectin 4 / Q000737:chemistry* / Q000302:isolation & purification; D006801:Humans
D002241:Carbohydrates; D037541:Galectin 4
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