Document Type
Article
Publication Date
1-1-2010
Abstract
Mannose-binding lectin from champedak (Artocarpus integer) is a homotetramer with a single-monomer molecular weight of 16 800 Da. Previous work has shown it to bind IgE and IgM, as well as being a mitogen of T cells in humans. Champedak mannose-binding lectin has successfully been used to detect altered glycosylation states of serum proteins. The protein was crystallized at 293 K in space group P2(1)2(1)2(1) (unit-cell parameters a = 76.89, b = 86.22, c = 95.37 angstrom) and the crystals diffracted to 2.0 angstrom resolution.
Keywords
lectins, Artocarpus integer, champedak, mannose binding.
Publication Title
Acta Crystallographica Section F-Structural Biology and Crystallization Communications
ISSN
1744-3091
Recommended Citation
Gabrielsen, M.; Abdul-Rahman, P.S.; Isaacs, N.W.; Hashim, Onn Haji; and Cogdell, R.J., "Crystallization and initial X-ray diffraction analysis of a mannose-binding lectin from champedak" (2010). Research Publications (2006 to 2010). 4330.
https://knova.um.edu.my/research_publications_2006_2010/4330
Divisions
fac_med
Volume
66
Issue
5
Additional Information
Gabrielsen, Mads Abdul-Rahman, Puteri Shafinaz Isaacs, Neil W. Hashim, Onn Haji Cogdell, Richard J. Part 5