Crystallization and initial X-ray diffraction analysis of a mannose-binding lectin from champedak

Gabrielsen, M. and Abdul-Rahman, P.S. and Isaacs, N.W. and Hashim, Onn Haji and Cogdell, R.J. (2010) Crystallization and initial X-ray diffraction analysis of a mannose-binding lectin from champedak. Acta Crystallographica Section F-Structural Biology and Crystallization Communications, 66 (5). pp. 592-594. ISSN 1744-3091, DOI https://doi.org/10.1107/s1744309110011760.

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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.

Item Type:	Article
Funders:	UNSPECIFIED
Additional Information:	Gabrielsen, Mads Abdul-Rahman, Puteri Shafinaz Isaacs, Neil W. Hashim, Onn Haji Cogdell, Richard J. Part 5
Uncontrolled Keywords:	lectins; Artocarpus integer; champedak; mannose binding.
Subjects:	R Medicine
Divisions:	Faculty of Medicine
Depositing User:	Ms Haslinda Lahuddin
Date Deposited:	10 Jul 2012 01:12
Last Modified:	24 Oct 2019 08:25
URI:	http://eprints.um.edu.my/id/eprint/3434

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