NDLI: Collectin structure: a review.

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Collectin structure: a review.

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Collectin structure: a review.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Håkansson, K. Reid, K. B.
Description	Country affiliation: United States Author Affiliation: Håkansson K ( Department of Microbiology, University of Illinois at Urbana-Champaign, Urbana 61801, USA. kjell@scs.uiuc.edu)
Abstract	Collectins are animal calcium dependent lectins that target the carbohydrate structures on invading pathogens, resulting in the agglutination and enhanced clearance of the microorganism. These proteins form trimers that may assemble into larger oligomers. Each polypeptide chain consists of four regions: a relatively short N-terminal region, a collagen like region, an alpha-helical coiled-coil, and the lectin domain. Only primary structure data are available for the N-terminal region, while the most important features of the collagen-like region can be derived from its homology with collagen. The structures of the alpha-helical coiled-coil and the lectin domain are known from crystallographic studies of mannan binding protein (MBP) and lung surfactant protein D (SP-D). Carbohydrate binding has been structurally characterized in several complexes between MBP and carbohydrate; all indicate that the major interaction between carbohydrate and collectin is the binding of two adjacent carbohydrate hydroxyl group to a collectin calcium ion. In addition, these hydroxyl groups hydrogen bond to some of the calcium amino acid ligands. While each collectin trimer contains three such carbohydrate binding sites, deviation from the overall threefold symmetry has been demonstrated for SP-D, which may influence its binding properties. The protein surface between the three binding sites is positively charged in both MBP and SP-D.
ISSN	09618368
e-ISSN	1469896X
Journal	Protein Science
Issue Number	9
Volume Number	9
Language	English
Publisher	Wiley-Blackwell (on behalf of The Protein Society)
Publisher Date	2000-09-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Carrier Proteins Chemistry Amino Acid Sequence Collectins Models, Molecular Molecular Sequence Data Protein Conformation Sequence Homology, Amino Acid Discipline Biochemistry
Content Type	Text
Resource Type	Article
Subject	Medicine Molecular Biology Biochemistry

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