Τίτλος:
Sequence patterns mediating functions of disordered proteins
Γλώσσες Τεκμηρίου:
Αγγλικά
Περίληψη:
Disordered proteins lack specific 3D structure in their native state and have been implicated with numerous cellular functions as well as with the induction of severe diseases, e.g., cardiovascular and neurodegenerative diseases as well as diabetes. Due to their conformational flexibility they are often found to interact with a multitude of protein molecules; this one-to-many interaction which is vital for their versatile functioning involves short consensus protein sequences, which are normally detected using slow and cumbersome experimental procedures. In this work we exploit information from disorder-oriented protein interaction networks focused specifically on humans, in order to assemble, by means of overrepresentation, a set of sequence patterns that mediate the functioning of disordered proteins; hence, we are able to identify how a single protein achieves such functional promiscuity. Next, we study the sequential characteristics of the extracted patterns, which exhibit a striking preference towards a very limited subset of amino acids; specifically, residues leucine, glutamic acid, and serine are particularly frequent among the extracted patterns, and we also observe a nontrivial propensity towards alanine and glycine. Furthermore, based on the extracted patterns we set off to infer potential functional implications in order to verify our findings and potentially further extrapolate our knowledge regarding the functioning of disordered proteins. We observe that the extracted patterns are primarily involved with regulation, binding and posttranslational modifications, which constitute the most prominent functions of disordered proteins. © Springer International Publishing Switzerland 2015.
Συγγραφείς:
Exarchos, K.P.
Kourou, K.
Exarchos, T.P.
Papaloukas, C.
Karamouzis, M.V.
Fotiadis, D.I.
Περιοδικό:
Advances in Experimental Medicine and Biology
Εκδότης:
Springer New York LLC
Λέξεις-κλειδιά:
glutamic acid; intrinsically disordered protein; leucine; serine; protein; protein binding, acylation; adenosine diphosphate ribosylation; adenylation; amidation; amino acid sequence; Article; binding affinity; carboxylation; glycosylation; human; molecular dynamics; prenylation; protein acetylation; protein analysis; protein binding; protein cleavage; protein database; protein function; protein motif; protein phosphorylation; protein processing; protein protein interaction; protein structure; protein synthesis; signal transduction; sulfation; ubiquitination; algorithm; chemical structure; chemistry; metabolism; molecular genetics; protein conformation; protein protein interaction, Algorithms; Amino Acid Sequence; Humans; Models, Molecular; Molecular Sequence Data; Protein Binding; Protein Conformation; Protein Interaction Maps; Proteins
DOI:
10.1007/978-3-319-09012-2_3
