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3 April 2000
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Cover Image
Cover picture: Ribbon diagram of the three-dimensional structure of the cysteine-rich domain of the mannose receptor (MR) complexed with a sulfated carbohydrate ligand. MR is a prototype member of a family of multilectin receptors that recognize carbohydrates on the cell walls of infectious organisms. The NH2-terminal cysteine-rich domain (Cys-MR) binds to glycoproteins containing sulfated sugars, such as sulfated hormones, and to chondroitin sulfates A and B and sulfated oligosaccharides of the Lewisa and Lewisx types. See related articles in this issue by Liu et al., 1105-1115, and Leteux et al., 1117-1126. - PDF Icon PDF LinkTable of Contents
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ISSN 0022-1007
EISSN 1540-9538
In this Issue
Article
The Cysteine-Rich Domain of the Macrophage Mannose Receptor Is a Multispecific Lectin That Recognizes Chondroitin Sulfates a and B and Sulfated Oligosaccharides of Blood Group Lewisa and Lewisx Types in Addition to the Sulfated N-Glycans of Lutropin
Christine Leteux,Wengang Chai,R. Wendy Loveless,Chun-Ting Yuen,Lars Uhlin-Hansen,Yves Combarnous,Mila Jankovic,Svetlana C. Maric,Ziva Misulovin,Michel C. Nussenzweig,Ten Feizi
Modulation of the Major Histocompatibility Complex Class II–Associated Peptide Repertoire by Human Histocompatibility Leukocyte Antigen (Hla)-Do
Marieke van Ham,Marcel van Lith,Björn Lillemeier,Esther Tjin,Ulrike Grüneberg,Dinah Rahman,Liesbeth Pastoors,Krista van Meijgaarden,Corinne Roucard,John Trowsdale,Tom Ottenhoff,Darryl Pappin,Jacques Neefjes
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