C-type lectin-like domains

Current Opinion in Structural Biology

Volumn 9, Issue 5, 1999, Pages 585-590

  Drickamer, Kurt ^a  

^a UNIVERSITY OF OXFORD   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM ION; LECTIN; LIGAND; OLIGOSACCHARIDE;

BINDING SITE; CALCIUM BINDING; EVOLUTION; MOLECULAR RECOGNITION; OLIGOMERIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN DOMAIN; REVIEW;

ANIMALIA;

EID: 0032860314     PISSN: 0959440X     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0959-440X(99)00009-3     Document Type: Review

References (33)

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19. •].
20. •], reveals secondary subsites that increase selectivity and affinity for saccharide ligands in C-type carbohydrate-recognition domains.
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24. 2+-binding sites in this C-type lectin-like domain and a surface that may interact with the surface of water crystals is identified.
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27. 2+ in maintaining the structure of a C-type carbohydrate-recognition domain.
28. 2+-binding site was analysed using fluorescence methods. This isomerisation may limit the rate of gain and loss of ligand-binding activity of carbohydrate-recognition domains during processes such as receptor-mediated endocytosis.
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