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Título

The eight-cysteine motif, a versatile structure in plant proteins

AutorJosé Estanyol, Matilde ; Gomis-Rüth, F. Xavier ; Puigdomènech, Pere
Palabras claveCereal protease inhibitors
Eight-cysteine motif
HyPRPs
LTPs
2S-albumins
Fecha de publicaciónmay-2004
EditorElsevier
CitaciónPlant Physiology and Biochemistry 42(5): 355-365 (2004)
ResumenA number of protein sequences deduced from the molecular analysis of plant cDNA or genomic libraries can be grouped in relation to a defined number of cysteine residues located in distinct positions of their sequences. This is the case for a group of around 500 polypeptides from different species that contain a small domain (less than 100 amino acids residues) displaying a pattern of eight-cysteines in a specific order. The plant sequences containing this motif belong to proteins having different functions, ranging from storage, protection, enzyme inhibition and lipid transfer, to cell wall structure. The eight-cysteine motif (8CM) appears to be a structural scaffold of conserved helical regions connected by variable loops, as observed by three-dimensional structure analysis. It is proposed that the cysteine residues would form a network of disulfide bridges necessary, for the maintenance of the tertiary structure of the molecule together with the central helical core, while the variable loops would provide the sequences required for the specific functions of the proteins. © 2004 Elsevier SAS. All rights reserved.
Versión del editorhttp://dx.doi.org/10.1016/j.plaphy.2004.03.009
URIhttp://hdl.handle.net/10261/107804
DOI10.1016/j.plaphy.2004.03.009
Identificadoresdoi: 10.1016/j.plaphy.2004.03.009
issn: 0981-9428
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