Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates
about
Plasticity in protein-peptide recognition: crystal structures of two different peptides bound to concanavalin A.Non-discriminating and discriminating aspartyl-tRNA synthetases differ in the anticodon-binding domainA novel crystal form of pyrrolysyl-tRNA synthetase reveals the pre- and post-aminoacyl-tRNA synthesis conformational states of the adenylate and aminoacyl moieties and an asparagine residue in the catalytic sitePlasmodial aspartyl-tRNA synthetases and peculiarities in Plasmodium falciparumCrystal structures of apo wild-type M. jannaschii tyrosyl-tRNA synthetase (TyrRS) and an engineered TyrRS specific for O-methyl-L-tyrosine.Modeling the binding sites of anti-hen egg white lysozyme antibodies HyHEL-8 and HyHEL-26: an insight into the molecular basis of antibody cross-reactivity and specificityIdentification of amino acids in the N-terminal domain of atypical methanogenic-type Seryl-tRNA synthetase critical for tRNA recognition.Emergence and evolution.Crystallization and preliminary X-ray crystallographic analysis of a bacterial Asn-transamidosome.Crystallization and preliminary X-ray crystallographic study of a putative aspartyl-tRNA synthetase from the crenarchaeon Sulfolobus tokodaii strain 7.Idiosyncratic helix-turn-helix motif in Methanosarcina barkeri seryl-tRNA synthetase has a critical architectural role.The crystal structure of archaeal nascent polypeptide-associated complex (NAC) reveals a unique fold and the presence of a ubiquitin-associated domain.Molecular Dynamics Simulations Show That Bound Mg2+Contributes to Amino Acid and Aminoacyl Adenylate Binding Specificity in Aspartyl-tRNA Synthetase through Long Range Electrostatic Interactions
P2860
Q27631967-B5A1DFB4-B4A2-49FB-9109-17FFA1A636EFQ27640832-2BE58323-9D59-4018-82EF-949B5574A957Q27683661-2A96EA53-FBAF-4DE3-B888-CB2464B3F8F8Q27972537-5ED7D5D2-0A26-4A8A-BF0C-0CA94148F0F7Q33214237-045FF9F3-F1B0-403D-90E7-14D754227169Q34183601-E711088C-EDC2-436C-883B-7C397EFBB7CAQ37431849-D5A8C24F-36BE-4A96-B5B7-B89F9BDA72B8Q38088164-0F284DE6-16BE-4040-9530-7BE6425D47BFQ40514346-66798960-5636-4537-A98F-CBD0694ECCA3Q41846592-C0BDB696-A58C-49E1-8F4B-69302AA1D71FQ43147159-AAE8AD16-0819-4345-B76F-1041C4412A20Q52940600-897424E4-900E-45EE-B02E-5673A4C3A527Q57077677-26C72B73-B487-4CD1-AAA6-B3CD63E26073
P2860
Aspartyl tRNA-synthetase from Escherichia coli: flexibility and adaptability to the substrates
description
2000 nî lūn-bûn
@nan
2000 թուականի Յունիսին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունիսին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Aspartyl tRNA-synthetase from ...... adaptability to the substrates
@ast
Aspartyl tRNA-synthetase from ...... adaptability to the substrates
@en
Aspartyl tRNA-synthetase from ...... adaptability to the substrates
@nl
type
label
Aspartyl tRNA-synthetase from ...... adaptability to the substrates
@ast
Aspartyl tRNA-synthetase from ...... adaptability to the substrates
@en
Aspartyl tRNA-synthetase from ...... adaptability to the substrates
@nl
prefLabel
Aspartyl tRNA-synthetase from ...... adaptability to the substrates
@ast
Aspartyl tRNA-synthetase from ...... adaptability to the substrates
@en
Aspartyl tRNA-synthetase from ...... adaptability to the substrates
@nl
P2093
P356
P1476
Aspartyl tRNA-synthetase from ...... adaptability to the substrates
@en
P2093
P304
P356
10.1006/JMBI.2000.3792
P407
P577
2000-06-23T00:00:00Z