Local structural motifs in proteins: Detection and characterization of fragments inserted in helices(12 visite) Balasco N, Smaldone G, Ruggiero A, De Simone A, Vitagliano L
Int J Biol Macromol (ISSN: 0141-8130linking, 1879-0003electronic), 2018 Oct 15; 118(PtB): 1924-1930.
Tipo di articolo: Journal Article,
Impact factor: 3.909, Impact factor a 5 anni: 3.227
Url: Non disponibile.
Parole chiave: Glycine Residue, Helix Insertion, Protein Stability, Ramachandran Space,
Affiliazioni:
*** IBB - CNR *** Institute of Biostructures and Bioimaging, C.N.R., Naples, Italy. Electronic address: nicole.balasco@unicampania.it. IRCCS SDN, Via Emanuele Gianturco 113, Naples, Italy. Division of Molecular Biosciences, Imperial College South Kensington Campus, London SW7 2AZ, UK.
Riferimenti:
Non disponibile.
The global/local fold of protein structures is stabilized by a variety of specific interactions. A primary role in this context is played by hydrogen bonds. In order to identify novel motifs in proteins, we searched Protein Data Bank structures looking for backbone H-bonds formed by NH groups of two (or more) consecutive residues with consecutive CO groups of distant residues in the sequence. The present analysis unravels the occurrence of recurrent structural motifs that, to the best of our knowledge, had not been characterized in literature. Indeed, these H-bonding patterns are found (i) in a specific parallel beta-sheet capping, (ii) in linking of beta-hairpins to alpha-helices, and (iii) in alpha-helix insertions. Interestingly, structural analyses of these motifs indicate that Gly residues frequently occupy prominent positions. The formation of these motifs is likely favored by the limited propensity of Gly to be embodied in helices/sheets. Of particular interest is the motif corresponding to insertions in helices that was detected in 1% of analyzed structures. Inserted fragments may assume different structures and aminoacid compositions and usually display diversified evolutionary conservation. Since inserted regions are physically separated from the rest of the protein structure, they represent hot spots for ad-hoc protein functionalization.<br>
Aloj L, Aurilio M, Rinaldi V, D'Ambrosio L, Tesauro D, Peitl PK, Maina T, Mansi R, Von Guggenberg E, Joosten L, Sosabowski JK, Breeman WA, De Blois E, Koelewijn S, Melis M, Waser B, Beetschen K, Reubi JC, De Jong M * The EEE project(111 visite) Proc Int Cosm Ray Conf Icrc Universidad Nacional Autonoma De Mexico, 2007; 5(HEPART2): 977-980. Impact Factor:0 DettagliEsporta in BibTeXEsporta in EndNote
95 Records (93 escludendo Abstract e Conferenze). Impact factor totale: 353.742 (347.544 escludendo Abstract e Conferenze). Impact factor a 5 anni totale: 363.397 (356.323 escludendo Abstract e Conferenze).
ibb.cnr.it