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Science 13 December 1991:
Vol. 254. no. 5038, pp. 1608 - 1615
DOI: 10.1126/science.1721241
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Articles

Science, Vol 254, Issue 5038, 1608-1615
Copyright © 1991 by American Association for the Advancement of Science

articles

Structure of the calcium-dependent lectin domain from a rat mannose-binding protein determined by MAD phasing

WI Weis, R Kahn, R Fourme, K Drickamer, and WA Hendrickson

Department of Biochemistry and Molecular Biophysics, Columbia University, New York, NY 10032.

Calcium-dependent (C-type) animal lectins participate in many cell surface recognition events mediated by protein-carbohydrate interactions. The C-type lectin family includes cell adhesion molecules, endocytic receptors, and extracellular matrix proteins. Mammalian mannose-binding proteins are C-type lectins that function in antibody-independent host defense against pathogens. The crystal structure of the carbohydrate-recognition domain of a rat mannose-binding protein, determined as the holmium-substituted complex by multiwavelength anomalous dispersion (MAD) phasing, reveals an unusual fold consisting of two distinct regions, one of which contains extensive nonregular secondary structure stabilized by two holmium ions. The structure explains the conservation of 32 residues in all C-type carbohydrate-recognition domains, suggesting that the fold seen here is common to these domains. The strong anomalous scattering observed at the Ho LIII edge demonstrates that traditional heavy atom complexes will be generally amenable to the MAD phasing method.


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