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001-es BibID:	BIBFORM050899
035-os BibID:	PMID:24044430 Article ID: 275
Első szerző:	Mótyán János András (biokémikus, molekuláris biológus)
Cím:	A molecular model of the full-length human NOD-like receptor family CARD domain containing 5 (NLRC5) protein / János András Mótyán, Péter Bagossi, Szilvia Benkő, József Tőzsér
Dátum:	2013
ISSN:	1471-2105
Megjegyzések:	Pattern recognition receptors of the immune system have key roles in the regulation of pathways after the recognition of microbial- and danger-associated molecular patterns in vertebrates. Members of NOD-like receptor (NLR) family typically function intracellularly. The NOD-like receptor family CARD domain containing 5 (NLRC5) is the largest member of this family that also contains the largest number of leucine-rich repeats (LRRs).Due to the lack of crystal structures of full-length NLRs, projects have been initiated with the aim to model certain or all members of the family, but systematic studies did not model the full-length NLRC5 due to its unique domain architecture.Our aim was to analyze the LRR sequences of NLRC5 and some NLRC5-related proteins and to build a model for the full-length human NLRC5 by homology modeling. RESULTS: LRR sequences of NLRC5 were aligned and were compared with the consensus pattern of ribonuclease inhibitor protein (RI)-like LRR subfamily. Two types of alternating consensus patterns previously identified for RI repeats were also found in NLRC5. A homology model for full-length human NLRC5 was prepared and, besides the closed conformation of monomeric NLRC5, a heptameric platform was also modeled for the opened conformational NLRC5 monomers. CONCLUSIONS: Identification of consensus patterns of leucine-rich repeat sequences helped to identify LRRs in NLRC5 and to predict their number and position within the protein. In spite of the lack of fully adequate template structures, the presence of an untypical CARD domain and unusually high number of LRRs in NLRC5, we were able to construct a homology model for both the monomeric and homo-heptameric full-length human NLRC5 protein.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban NLRC5 Molecular modeling LRR protein NOD-like receptor
Megjelenés:	BMC Bioinformatics 14 : 1 (2013), p. 1-11. -
További szerzők:	Bagossi Péter (1966-2011) (biokémikus, vegyész) Benkő Szilvia (1973-) (molekuláris biológus) Tőzsér József (1959-) (molekuláris biológus, biokémikus, vegyész)
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001-es BibID:	BIBFORM018946
Első szerző:	Mótyán János András (biokémikus, molekuláris biológus)
Cím:	Transglycosylation by barley alfa-amylase 1 / Mótyán János A., Fazekas Erika, Mori Haruhide, Svensson Birte, Bagossi Péter, Kandra Lili, Gyémánt Gyöngyi
Dátum:	2011
ISSN:	1381-1177
Megjegyzések:	The transglycosylation activity of barley alfa-amylase 1 (AMY1) and active site AMY1 subsite mutant enzymes was investigated. We report here the transferase ability of the V47A, V47F, V47D and S48Y single mutants and V47K/S48G and V47G/S48D double mutant AMY1 enzymes in which the replaced amino acids play important role in substrate binding at subsites at-3 through-5. Although mutation increases the transglycosylation activity of enzymes, in the presence of acceptors the difference between wild type and mutants is not so significant. Oligomer transfer reactions of AMY1 wild type and its mutants were studied using maltoheptaose and maltopentaose donors and different chromophore containing acceptors. The conditions for the chemoenzymatic synthesis of 4-methylumbelliferyl-alfa-d-maltooligosaccharides (MU-alfa-d-MOSs) were optimized using 4-methylumbelliferyl-alfa-d-glucoside as acceptor and maltoheptaose as donor. 4-Methylumbelliferyl-alfa-d-maltoside, -maltotrioside, -maltotetraoside and -maltopentaoside have been synthesized. Products were identified by MALDI-TOF MS. 1H and 13C NMR analyses showed that AMY1 V47F preserved the stereo- and regioselectivity. The produced MU-alfa-d-MOSs of degree of polymerization DP 2, DP 3 and DP 5 were successfully applied to detect activity of Bacillus stearothermophilus maltogenic alfa-amylase, human saliv
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Barley alpha-amylase 1 Transglycosylation Methylumbelliferyl-glycosides Chemoenzymatic synthesis Amylase assay
Megjelenés:	Journal Of Molecular Catalysis B-Enzymatic. - 72 : 3-4 (2011), p. 229-237. -
További szerzők:	Fazekas Erika (1985-) (kémikus) Mori, Haruhide Svensson, Birte Bagossi Péter (1966-2011) (biokémikus, vegyész) Kandra Lili (1943-) (biokémikus) Gyémánt Gyöngyi (1960-) (vegyész)
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001-es BibID:	BIBFORM013253
Első szerző:	Mótyán János András (biokémikus, molekuláris biológus)
Cím:	Computer-aided subsite mapping of alpha-amylases / János A. Mótyán, Gyöngyi Gyémánt, János Harangi, Péter Bagossi
Dátum:	2011
Megjegyzések:	Subsite mapping is a crucial procedure in the characterization of alpha-amylases (EC 3.2.1.1), which are extensively used in starch-based industries and in diagnosis of pancreatic and salivary glands disorders. A computer-aided method has been developed for subsite mapping of alpha-amylases, which substitutes the difficult, expensive, and time-consuming experimental determination of action patterns to crystal structures based energy calculations. Interaction energies between enzymes and carbohydrate substrates were calculated after short energy minimization by a molecular mechanics program. A training set of wild type and mutant amylases with known experimental action patterns of 13 enzymes of wide range of origin was used to set up the procedure. Calculations for training set resulted in good correlation in case of subsite binding energies (r2 = 0.827-0.929) and bond cleavage frequencies (r2 = 0.727-0.835). A set of eight novel barley amylase 1 mutants was used to test our model. Subsite binding energies were predicted with r2 = 0.502 correlation coefficient, while bond cleavage frequency prediction resulted in r2 = 0.538. Our computer-aided procedure may supplement the experimental subsite mapping methods to predict and understand characteristic features of alpha-amylases.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban alpha-amylase subsite mapping binding energy bond cleavage frequency molecular modeling
Megjelenés:	Carbohydrate Research. - 346 : 3 (2011), p. 410-415. -
További szerzők:	Gyémánt Gyöngyi (1960-) (vegyész) Harangi János (1950-) (biokémikus, kromatográfus) Bagossi Péter (1966-2011) (biokémikus, vegyész)
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