LitCovid-sentences  

PMC:7094172 / 5756-8570 JSONTXT 14 Projects

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Id Subject Object Predicate Lexical cue
T38 0-80 Sentence denotes Figure 1B shows the details of the interactions in the MERS-CoV N protein dimer.
T39 81-136 Sentence denotes We named the units monomer 1 and monomer 2 (Figure 1A).
T40 137-367 Sentence denotes According to the amino acid composition of the binding site on monomer 2, we divided the dimeric interface into two areas: one located on the N-terminus flexible region and the other on the loop between β4 and β5 of the N protein.
T41 368-575 Sentence denotes In the first area, W43, N66, N68, Y102, and F135 of monomer 1 generated a conserved hydrophobic pocket permitting the side chain of M38 of monomer 2 to enter this hole by a hydrophobic contact (Figure 1C,D).
T42 576-709 Sentence denotes H37 and N39 of monomer 2 were packed against W43 and F135 of monomer 1, respectively, and contributed to the hydrophobic interaction.
T43 710-829 Sentence denotes The side chains of N39 of monomer 2 formed one hydrogen bond with the N68 backbone in monomer 1 at a distance of 2.6 Å.
T44 830-878 Sentence denotes The second area was relatively more hydrophilic.
T45 879-1067 Sentence denotes The main chain oxygens of G104, F135, and T137 of monomer 2 formed three hydrogen bonds with the side chains of Q73 and T134 of monomer 1 at distances of 3.8, 3.2, and 3.7 Å, respectively.
T46 1068-1198 Sentence denotes The side chain of N139 on monomer 2 formed a hydrogen bond with the main chain oxygen of T137 on monomer 1 at a distance of 3.6 Å.
T47 1199-1314 Sentence denotes The interactions of the first and second areas comprise buried surface areas (BSA) of 289 and 103 Å2, respectively.
T48 1315-1462 Sentence denotes The small surface area buried at the interface accounts for ∼5 kcal mol–1 binding energy,26 which translates to a dissociation constant of ∼200 mM.
T49 1463-1611 Sentence denotes Thus, the dimer described here is unique in that it is non-native and relies on vector-fusion residues (H37 and M38) to maintain its dimeric status.
T50 1612-1904 Sentence denotes This property may also explain why the present structure has an oligomeric status different from previously reported structures for the CoV N protein.24,27−30 We used cross-linking experiments to analyze the oligomeric capacity of MERS N-NTD containing the vector-fusion residues in solution.
T51 1905-1955 Sentence denotes MERS N-NTD had a dimeric conformation in solution.
T52 1956-2140 Sentence denotes Our structure indicated that W43 played an essential role in forming the hydrophobic pocket accommodating the vector-fusion residues and, therefore, mediated the N-NTD dimer formation.
T53 2141-2227 Sentence denotes The W43A mutation significantly reduced the oligomeric tendency of N-NTD (Figure S1C).
T54 2228-2358 Sentence denotes This further supports that the “exogenous residues” encoded by the vector backbone mediated the formation of the non-native dimer.
T55 2359-2441 Sentence denotes We also superimposed the previously published structure of MERS-CoV N-NTD (PDB ID:
T56 2442-2522 Sentence denotes 4ud1)27 containing a native N-terminal flexible region with our dimer structure.
T57 2523-2668 Sentence denotes The side chain of N38 in the native structure could not interact with the hydrophobic pocket as the former is hydrophilic and short (Figure S1E).
T58 2669-2814 Sentence denotes Thus, it may be possible to utilize small compounds to replace the vector-fusion residues and stabilize the PPI through hydrophobic interactions.