Crystallization and preliminary crystallographic data of a neutrophil migration-inducing lectin (KM+) extracted from the seed ofArtocarpus integrifolia

The structure of Heltuba, which is the prototype for an extended family of mannose-binding agglutinins, shares the carbohydrate-binding site and beta-prism topology of its galactose-binding counterparts jacalin and Maclura pomifera lectin. However, the beta-prism elements recruited to form the octameric interface of Heltuba, and the strategy used to forge the mannose-binding site, are unique and markedly dissimilar to those described for jacalin. The present structure highlights a hitherto unrecognized adaptability of the beta-prism building block in the evolution of plant proteins.

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Oliveira¹,

Garratt²

1998

Journal of Computer-Aided Molecular Design

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We describe the application of a method for the reconstruction of three-dimensional atomic co-ordinates from a stereo ribbon diagram of a protein when additional information for some of the sidechain positions is available. The method has applications in cases where the 3D co-ordinates have not been made available by any means other than the original publication and are of interest as models for molecular replacement, homology modelling etc. The approach is, on the one hand, more general than other methods which are based on stereo figures which present specific atomic positions, but on the other hand relies on input from a specialist. Its exact implementation will depend on the figure of interest. We have applied the method to the case of the alpha-D-galactose-binding lectin jacalin with a resultant RMS deviation, compared to the crystal structure, of 1.5 A for the 133 C alpha positions of the alpha-chain and 2.6 A for the less regular beta-chain. The success of the method depends on the secondary structure of the protein under consideration and the orientation of the stereo diagram itself but can be expected to reproduce the mainchain co-ordinates more accurately than the sidechains. Some ways in which the method may be generalised to other cases are discussed.

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Crystallization and preliminary crystallographic data of a neutrophil migration-inducing lectin (KM+) extracted from the seed ofArtocarpus integrifolia

Cited by 4 publications

References 6 publications

Structural and thermodynamic studies of KM+, a d-mannose binding lectin from Artocarpus integrifolia seeds

Structural and thermodynamic studies of KM+, a d-mannose binding lectin from Artocarpus integrifolia seeds

Helianthus tuberosus lectin reveals a widespread scaffold for mannose-binding lectins

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