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Crystallization and Initial X-ray Diffraction Analysis of a Mannose-binding Lectin from Champedak

Overview
Journal Acta Crystallogr Sect F Struct Biol Cryst Commun
Date 2010 May 7
PMID 20445267
Citations 2
Authors
Mads Gabrielsen
Puteri Shafinaz Abdul-Rahman
Neil W Isaacs
Onn Haji Hashim
Richard J Cogdell
Affiliations
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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 A) and the crystals diffracted to 2.0 A resolution.

Citing Articles

Overview of the Structure⁻Function Relationships of Mannose-Specific Lectins from Plants, Algae and Fungi.

Barre A, Bourne Y, Van Damme E, Rouge P Int J Mol Sci. 2019; 20(2).

PMID: 30634645 PMC: 6359319. DOI: 10.3390/ijms20020254.

Structures and binding specificity of galactose- and mannose-binding lectins from champedak: differences from jackfruit lectins.

Gabrielsen M, Abdul-Rahman P, Othman S, Hashim O, Cogdell R Acta Crystallogr F Struct Biol Commun. 2014; 70(Pt 6):709-16.

PMID: 24915077 PMC: 4051521. DOI: 10.1107/S2053230X14008966.

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