Journal article
In silico determination of intracellular glycosylation and phosphorylation sites in human selectins: Implications for biological function
Post-translational modifications provide the proteins with the possibility to perform functions in addition to those determined by their primary sequence. However, analysis of multifunctional protein structures in the environment of cells and body fluids is made especially difficult by the presence of other interacting proteins.
Bioinformatics tools are therefore helpful to predict protein multifunctionality through the identification of serine and threonine residues wherein the hydroxyl group is likely to become modified by phosphorylation or glycosylation. Moreover, serines and threonines where both modifications are likely to occur can also be predicted (YinYang sites), to suggest further functional versatility.
Structural modifications of hydroxyl groups of P-, E-, and L-selectins have been predicted and possible functions resulting from such modifications are proposed. Functional changes of the three selectins are based on the assumption that transitory and reversible protein modifications by phosphate and O-GlcNAc cause specific conformational changes and generate binding sites for other proteins.
The computer-assisted prediction of glycosylation and phosphorylation sites in selectins should be helpful to assess the contribution of dynamic protein modifications in selectin-mediated inflammatory responses and cell-cell adhesion processes that are difficult to determine experimentally. J. Cell.
Biochem. 100: 1558-1572, 2007.
Language: | English |
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Publisher: | Wiley Subscription Services, Inc., A Wiley Company |
Year: | 2007 |
Pages: | 1558-1572 |
ISSN: | 10974644 , 07302312 and 07331959 |
Types: | Journal article |
DOI: | 10.1002/jcb.21156 |
ORCIDs: | Gupta, Ramneek |
YinYang sites glycosylation multifunctional proteins phosphorylation post-translational modifications
Algorithms Amino Acid Sequence Computational Biology Databases, Protein E-Selectin Glycosylation Humans L-Selectin Models, Biological Models, Molecular Molecular Sequence Data P-Selectin Phosphorylation Protein Processing, Post-Translational Protein Structure, Secondary Selectins Sequence Homology, Amino Acid