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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 macrophages

Authors
 Noella Silva-Martin  ;  Joseph D.Schauer  ;  Chae Gyu Park  ;  Juan A. Hermoso 
Citation
 ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS, Vol.65(pt 12) : 1264-1266, 2009 
Journal Title
 ACTA CRYSTALLOGRAPHICA SECTION F-STRUCTURAL BIOLOGY AND CRYSTALLIZATION COMMUNICATIONS 
Issue Date
2009
MeSH
Animals ; Antibodies/metabolism* ; CHO Cells ; Cell Adhesion Molecules/chemistry* ; Cell Adhesion Molecules/metabolism ; Cricetinae ; Cricetulus ; Crystallography, X-Ray ; Lectins, C-Type/chemistry* ; Lectins, C-Type/metabolism ; Macrophages/immunology ; Macrophages/metabolism* ; Mice ; Polysaccharides/metabolism* ; Protein Conformation ; Receptors, Cell Surface/chemistry* ; Receptors, Cell Surface/metabolism ; Recombinant Proteins/chemistry ; Recombinant Proteins/metabolism ; Spleen/immunology ; Spleen/metabolism*
Keywords
SIGN-R1 ; carbohydrate-recognition domains ; C-type lectin receptors
Abstract
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 A, beta = 121.66 degrees , allowed the collection of a full X-ray data set to a maximum resolution of 1.87 A.
Files in This Item:
T200906221.pdf Download
DOI
10.1107/S1744309109041992
Appears in Collections:
1. College of Medicine (의과대학) > BioMedical Science Institute (의생명과학부) > 1. Journal Papers
Yonsei Authors
Park, Chae Gyu(박채규) ORCID logo https://orcid.org/0000-0003-1906-1308
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/106078
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