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The molecular basis for both selective and flexible carbohydrate protein recognition

Obiettivo

Protein-carbohydrate recognition plays a critical role in many biological processes and the structural basis for the interaction of proteins with complex carbohydrates is poorly understood. The interaction of degradative enzymes with their target substrates within the plant cell wall provides an excellent model system in which carbohydrate protein recognition can be studied.

The determination of how proteins may exhibit selectivity for a specific type of polysaccharide, while at the same time displaying relaxed ligand specificity to accommodate the variation in the structure of the target carbohydrate polymers, provides important insights into both the selectivity and flexibility of protein carbohydrate recognition.

An elegant example of this plasticity in ligand recognition is the hydrolytic system that degrades mannose- containing polysaccharides. Mannanases and their associated carbohydrate binding modules (CBMs) display both remarkable specificity for O-manno-configured substrates but at the same time accommodate, to varying degrees, both homopolymers of mannose and heteropolymers of mannose and glucose whilst specifically excluding other polysaccharides.

The recognition of mannosides is central to a diverse array of current industrial and medical processes. Thus, the initial aim of this project is to elucidate the mechanisms by which mannanases and CBMs that recognise mannan and glucomannan recognise their respective substrates and ligands.

The understanding of the structural basis of the substrate specificity of these enzymes obtained in the initial phase of the project will inform and direct strategies designed to engineer novel specificity into these enzymes so that mannose-containing carbohydrates, tailor-made for specific applications can be synthesized. The data will make an important contribution to the fundamental basis of both selective and flexible specificity in protein-carbohydrate recognition.

Invito a presentare proposte

FP6-2002-MOBILITY-5
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Coordinatore

UNIVERSITY OF NEWCASTLE UPON TYNE
Contributo UE
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Indirizzo
6 Kensington Terrace
NEWCASTLE UPON TYNE
Regno Unito

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