Premium
Lessons from nature: On the molecular recognition elements of the phosphoprotein binding‐domains
Author(s) -
Roque A. Cecília A.,
Lowe Christopher R.
Publication year - 2005
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/bit.20561
Subject(s) - phosphoprotein , proteome , phosphorylation , computational biology , molecular recognition , identification (biology) , human proteome project , chemistry , proteomics , protein phosphorylation , biochemistry , biology , molecule , gene , botany , organic chemistry , protein kinase a
The reversible phosphorylation of proteins regulates many biological processes. Despite the technological advances in the enrichment and detection of phosphorylated proteins, the currently available techniques still struggle with the complexity of the human proteome. The aim of this review is to highlight the molecular recognition elements of the interaction between phosphorylated proteins and peptides and pTyr or pSer/Thr‐binding domains. The identification of the recognition features of the naturally occurring pTyr‐ and pSer/Thr‐binding domains can contribute to an understanding of the molecular aspects of the affinity and specificity for phosphorylated residues. This might inspire the design of small “biomimetic” molecules with potential applications in assessing the extent of the phosphoproteome using affinity‐based strategies. © 2005 Wiley Periodicals, Inc.