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PubMed:23633953 JSONTXT

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DisGeNET

Id Subject Object Predicate Lexical cue
T0 255-260 gene:7334 denotes Ubc13
T1 224-232 disease:C0013371 denotes Shigella
R1 T0 T1 associated_with Ubc13,Shigella

DisGeNET5_gene_disease

Id Subject Object Predicate Lexical cue
23633953-2#35#40#gene7334 255-260 gene7334 denotes Ubc13
23633953-2#66#71#gene7334 286-291 gene7334 denotes Ubc13
23633953-2#4#12#diseaseC0013371 224-232 diseaseC0013371 denotes Shigella
35#40#gene73344#12#diseaseC0013371 23633953-2#35#40#gene7334 23633953-2#4#12#diseaseC0013371 associated_with Ubc13,Shigella
66#71#gene73344#12#diseaseC0013371 23633953-2#66#71#gene7334 23633953-2#4#12#diseaseC0013371 associated_with Ubc13,Shigella

Inflammaging

Id Subject Object Predicate Lexical cue
T1 0-131 Sentence denotes Complex structure of OspI and Ubc13: the molecular basis of Ubc13 deamidation and convergence of bacterial and host E2 recognition.
T2 132-219 Sentence denotes Ubc13 is an important ubiquitin-conjugating (E2) enzyme in the NF-κB signaling pathway.
T3 220-377 Sentence denotes The Shigella effector OspI targets Ubc13 and deamidates Gln100 of Ubc13 to a glutamic acid residue, leading to the inhibition of host inflammatory responses.
T4 378-461 Sentence denotes Here we report the crystal structure of the OspI-Ubc13 complex at 2.3 Å resolution.
T5 462-603 Sentence denotes The structure reveals that OspI uses two differently charged regions to extensively interact with the α1 helix, L1 loop and L2 loop of Ubc13.
T6 604-680 Sentence denotes The Gln100 residue is bound within the hydrophilic catalytic pocket of OspI.
T7 681-917 Sentence denotes A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI.
T8 918-1173 Sentence denotes The OspI-binding sites in Ubc13 largely overlap with the binding residues for host ubiquitin E3 ligases and a deubiquitinating enzyme, which suggests that the bacterial effector and host proteins exploit the same surface on Ubc13 for specific recognition.
T9 1174-1427 Sentence denotes Biochemical results indicate that both of the differently charged regions in OspI are important for the interaction with Ubc13, and the specificity determinants in Ubc13 for OspI recognition reside in the distinct residues in the α1 helix and L2 region.
T10 1428-1570 Sentence denotes Our study reveals the molecular basis of Ubc13 deamidation by OspI, as well as a convergence of E2 recognition by bacterial and host proteins.
T1 0-131 Sentence denotes Complex structure of OspI and Ubc13: the molecular basis of Ubc13 deamidation and convergence of bacterial and host E2 recognition.
T2 132-219 Sentence denotes Ubc13 is an important ubiquitin-conjugating (E2) enzyme in the NF-κB signaling pathway.
T3 220-377 Sentence denotes The Shigella effector OspI targets Ubc13 and deamidates Gln100 of Ubc13 to a glutamic acid residue, leading to the inhibition of host inflammatory responses.
T4 378-461 Sentence denotes Here we report the crystal structure of the OspI-Ubc13 complex at 2.3 Å resolution.
T5 462-603 Sentence denotes The structure reveals that OspI uses two differently charged regions to extensively interact with the α1 helix, L1 loop and L2 loop of Ubc13.
T6 604-680 Sentence denotes The Gln100 residue is bound within the hydrophilic catalytic pocket of OspI.
T7 681-917 Sentence denotes A comparison between Ubc13-bound and wild-type free OspI structures revealed that Ubc13 binding induces notable structural reassembly of the catalytic pocket, suggesting that substrate binding might be involved in the catalysis of OspI.
T8 918-1173 Sentence denotes The OspI-binding sites in Ubc13 largely overlap with the binding residues for host ubiquitin E3 ligases and a deubiquitinating enzyme, which suggests that the bacterial effector and host proteins exploit the same surface on Ubc13 for specific recognition.
T9 1174-1427 Sentence denotes Biochemical results indicate that both of the differently charged regions in OspI are important for the interaction with Ubc13, and the specificity determinants in Ubc13 for OspI recognition reside in the distinct residues in the α1 helix and L2 region.
T10 1428-1570 Sentence denotes Our study reveals the molecular basis of Ubc13 deamidation by OspI, as well as a convergence of E2 recognition by bacterial and host proteins.