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001-es BibID:	BIBFORM003917
Első szerző:	Csősz Éva (biokémikus, molekuláris biológus)
Cím:	Substrate preference of transglutaminase 2 revealed by logistic regression analysis and intrinsic disorder examination / Csősz, É., Bagossi, P., Nagy, Z., Dosztányi, Zs., Simon, I., Fésüs, L.
Dátum:	2008
Megjegyzések:	Tissue transglutaminase (TG2) catalyzes the Ca(2+)-dependent posttranslational modification of proteins via formation of isopeptide bonds between their glutamine and lysine residues. Although substrate specificity of TG2 has been studied repeatedly at the sequence level, no clear consensus sequences have been determined so far. With the use of the extensive structural information on TG2 substrate proteins listed in TRANSDAB Wiki database, a slight preference of TG2 for glutamine and lysine residues situated in turns could be observed. When the spatial environment of the favored glutamine and lysine residues was analyzed with logistic regression, the presence of specific amino acid patterns was identified. By using the occurrence of the predictor amino acids as selection criteria, several polypeptides were predicted and later identified as novel in vitro substrates for TG2. By studying the sequence of TG2 substrate proteins lacking available crystal structure, the strong favorable influence on substrate selection of the presence of substrate glutamine and lysine residues in intrinsically disordered regions could also be revealed. The collected structural data have provided novel understanding of how this versatile enzyme selects its substrates in various cell compartments and tissues.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of Molecular Biology 383 : 2 (2008), p. 390-402. -
További szerzők:	Bagossi Péter (1966-2011) (biokémikus, vegyész) Nagy Zoltán (számítástechnikus) Dosztányi Zsuzsanna Simon István Fésüs László (1947-) (orvos biokémikus)
Internet cím:	elektronikus változat DOI
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