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Carbohydrate-recognition Domain (carbohydrate-recognition + domain)
Selected AbstractsExpression, purification, refolding and crystallization of the carbohydrate-recognition domain of p58/ERGIC-53, an animal C-type lectin involved in export of glycoproteins from the endoplasmic reticulumACTA CRYSTALLOGRAPHICA SECTION D, Issue 3 2002Lucas M. Velloso p58/ERGIC-53 is a mammalian calcium-dependent lectin that serves as a glycoprotein-sorting receptor between the endoplasmic reticulum (ER) and the Golgi complex. It is a type I transmembrane protein with two lumenal domains, one of which is a carbohydrate-recognition domain (CRD) and homologous to leguminous lectins. The CRD of p58, the rat homologue of human ERGIC-53, was overexpressed in insect cells and Escherichia coli, purified and crystallized using Li2SO4 as a precipitant. The crystals belong to space group I222, with unit-cell parameters a = 49.6, b = 86.1, c = 128.1,Å, and contain one molecule per asymmetric unit, corresponding to a packing density of 2.4,Å3,Da,1. Knowledge of the structure of p58/ERGIC-53 will provide a starting model for understanding receptor-mediated glycoprotein sorting between the ER and the Golgi. [source] Cloning, expression, purification, crystallization and preliminary X-ray diffraction analysis of the N-terminal carbohydrate-recognition domain of human galectin-4ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 5 2010Ana Lucia L. R. Zimbardi 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,Å resolution and the structure has been solved by the molecular-replacement technique. The crystals belonged to space group P6122, with unit-cell parameters a = b = 71.25, c = 108.66,Å. The asymmetric unit contained one molecule of hGal4-CRD-1, with a VM value of 2.34,Å3,Da,1 and a solvent content of 47.51%. [source] Crystallization and preliminary X-ray diffraction studies of the carbohydrate-recognition domain of SIGN-R1, a receptor for microbial polysaccharides and sialylated antibody on splenic marginal zone macrophagesACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 12 2009Noella Silva-Martin SIGN-R1, or CD209b, is a mouse C-type lectin receptor that is expressed at high levels on macrophages in lymphoid tissues, especially within the marginal zone of the spleen. SIGN-R1 can bind and mediate the uptake of various microbial polysaccharides, including dextrans, lipopolysaccharides and pneumococcal capsular polysaccharides. It has been shown that SIGN-R1 mediates the clearance of encapsulated pneumococcus, complement fixation via binding C1q independent of antibody and innate resistance to pneumococcal infection. Recently, SIGN-R1 has also been demonstrated to bind sialylated antibody and mediate its activity to suppress autoimmunity. The carbohydrate-recognition domain (CRD) of SIGN-R1 has been cloned and overexpressed in a soluble secretory form in mammalian Chinese hamster ovary (CHO) cells. The CRD protein of SIGN-R1 was purified from CHO cell-culture supernatant and concentrated for crystallization using the hanging-drop vapour-diffusion method at 291,K. Crystals grew from a mixture of 2,M ammonium sulfate in 0.1,M bis-tris pH 5.5. Single crystals, which belonged to the monoclinic space group C2 with unit-cell parameters a = 146.72, b = 92.77, c = 77.06,Å, , = 121.66°, allowed the collection of a full X-ray data set to a maximum resolution of 1.87,Å. [source] Crystallization of the head and galectin-like domains of porcine adenovirus isolate NADC-1 fibreACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 11 2009Pablo Guardado-Calvo The porcine adenovirus NADC-1 isolate, a strain of porcine adenovirus type 4, has a fibre with an atypical architecture. In addition to a classical virus-attachment region, shaft and head domains, it contains an additional galectin-like domain C-terminal to the head domain and connected to the head domain by a long RGD-containing loop. The galectin-like domain contains two putative carbohydrate-recognition domains. The head and galectin-like domains have been independently crystallized. Diffraction data have been obtained to 3.2,Å resolution from crystals of the head domain and to 1.9,Å resolution from galectin-like domain crystals. [source] Crystallization and preliminary X-ray diffraction analysis of a protease-resistant mutant form of human galectin-8ACTA CRYSTALLOGRAPHICA SECTION F (ELECTRONIC), Issue 5 2009Hiromi Yoshida A crystal of a protease-resistant mutant form of human galectin-8, a tandem-repeat-type galectin with two carbohydrate-recognition domains, was obtained using the hanging-drop method and was found to belong to the tetragonal space group P43212, with unit-cell parameters a = 78.93, b = 78.93, c = 132.05,Å. Diffraction data were collected to a resolution of 3.4,Å. [source] | ||||||||||