ライフサイエンスコーパス: paratope

1 rmed cleft using a convex binding interface (paratope).

2 only A2 contributes to the canonical Hib PS paratope.

3 ill" and VH "valley" shape of the grooved E8 paratope.

4 een this peptide and the monoclonal antibody paratope.

5 bclasses and IgA, consistent with an altered paratope.

6 icity with conformational versatility of the paratope.

7 sequence information on the location of the paratope.

8 nce-based information on the location of the paratope.

9 d in order to map the structural epitope and paratope.

10 al of 16 amino acid residues in the antibody paratope.

11 seven amino acids form part of the CAT-2200 paratope.

12 ed the affinity limit achievable with a flat paratope.

13 dues suggested that this is not an optimized paratope.

14 ties via their unusually long, convex-shaped paratopes.

15 es, mimicking the energetic core of antibody paratopes.

16 he minor portion of the predicted functional paratopes.

17 opes whose cognate mAbs have electropositive paratopes.

18 t a source for human antibodies with genuine paratopes.

19 nt in combination with other nonneutralizing paratopes.

20 m pneumococcal capsular PS (PPS) 6B-specific paratopes.

21 It also occurs when a flexible paratope accommodates dissimilar Ags by adjusting struct

22 ope is fixed while variation in the antibody paratope allows increasing affinity.

23 The epitope as defined by the IgE paratope and a set of chimeric Bet v 1 fusion proteins a

24 nt of SCV therapeutics based on the antibody paratope and epitope, and a retrovaccinology approach fo

25 remarkable feature revealed lies within the paratope and is a novel six-amino-acid alpha-helix that

26 Surprisingly, Tyr still dominates the YSX paratope and the additional amino acid types are primari

27 he antibody molecules reducing the hiding of paratopes, and (ii) maintained the activity of the captu

28 We suggest that the convex paratope antibody libraries described here could be read

29 ith orientation control for site-positioning paratopes (antigen binding site) of the antibody molecul

30 It is not clearly understood how the paratopes are able to recognize sequence-wise featureles

31 on average, complete structural epitopes and paratopes are equal in size to each other and similar in

32 The functional paratopes are surrounded by favorable polar atomistic co

33 site thus comprises antibodies with distinct paratopes arrayed about two optimal geometric orientatio

34 The peptide structures differed, and the two paratopes attained discrete conformations, leading to di

35 Although paratope chemistries differed, all 16 gp120-CD4bs antibo

36 ucture at 3.2 A resolution reveals a contact paratope composed almost entirely of tryptophan and seri

37 studies, the findings indicate that a hybrid paratope consisting of quinine and reconfigured antibody

38 , VH-V1a recognizes VEGF by using an unusual paratope consisting predominantly of CDR3 but with signi

39 Mapping the epitope-paratope contact interfaces revealed that these function

40 The key residues within the paratope contributing to binding were identified as Asp5

41 nd use a combination of structural analysis, paratope dissection, and neutralization assessment to de

42 e switching generated a surprising degree of paratope diversity within the individuals analyzed.

43 density comparisons were used to analyze the paratope-epitope interface and demonstrated that the ant

44 y identical charge interactions occur at all paratope-epitope interfaces.

45 e polar atomistic contacts in the structural paratope-epitope interfaces; more that 80% these polar c

46 sin may be limiting the accessible space for paratope evolution.

47 lonal within the individual, with one or two paratope families accounting for the majority of express

48 level, with the same two L-chain-determined paratope families recurring in all individuals.

49 Modeling demonstrates that the paratope forms a groove suitable for binding two beta-ri

50 othesize that the hydrophobic surface of the paratope functions as a "trap" for the viral sequences,

51 The functional paratope (hot spot) predictions on a set of 111 antibody

52 LIPH (grouping of lymphocyte interactions by paratope hotspots) to cluster TCRs with a high probabili

53 quence protected from proteolysis by the 2F5 paratope; (ii) downstream residues postulated to establi

54 y suggested direct involvement of a flexible paratope in the observed mimicry.

55 the size of a complete structural epitope or paratope, inclusive of CR and the minimum set of support

56 s could be used as specific non-covalent and paratope-independent handles in targeted drug delivery,

57 ntarity-determining regions that are driving paratope interactions; the variable light complementarit

58 antigen complex revealed that the structural paratope is dominated by Tyr side-chains.

59 nesis experiments reveal that the functional paratope is dominated by Tyr, which represents 11 of the

60 contact between the B2.1 peptide and the b12 paratope is unlikely to mimic the discontinuous key bind

61 finity is engineered outside of the antibody paratope, it can complement affinity maturation strategi

62 We chose a minimalist paratope limited to two loops found in a natural camelid

63 The paratope map of b12 may facilitate the design of molecul

64 ; (iii) antigen selection increased antibody paratope net charge and solvent-accessible surface area;

65 njugating a cholesterol group outside of the paratope of an antibody.

66 ubstitutions of selected residues to map the paratope of Fab 2F5.

67 ggesting that the peptides bind close to the paratope of the Ab.

68 an and tyrosine residues highly populate the paratope of the antibody but not the epitope of the anti

69 Instead, the paratope of the antibody undergoes a large conformationa

70 ction-linked (PL) biopanning," probes the Ab paratopes of protected vaccinees versus those with vacci

71 variability of antigenic epitopes, where the paratope on the antibody binds specifically to a given e

72 employed thiophene-3-boronic acid (T3BA) as paratope orientation controller, (i) enabled site orient

73 Structural characterization of epitope-paratope pairs has contributed to the understanding of a

74 ntibody binding-site composition at putative paratope positions.

75 We describe a paratope raised against the human ErbB family member HER

76 The amino acid composition of the paratope reflects the library diversity, consisting most

77 structurally important positions within the paratope region and (b) tailored amino acid composition

78 Structurally important positions within the paratope region were identified through stability, struc

79 finitive characterization of the epitope and paratope regions.

80 sity to the light chain, by diversifying non-paratope residues that may influence CDR conformations,

81 iding models for the interacting epitope and paratope residues.

82 ing potential developability issues; predict paratope residues; and predict epitope patches on protei

83 led molecular comparison of an anti-idiotype paratope specific for a human antibody with its analogou

84 traints on the variable (V) region to affect paratope structure in a V region identical IgG(1), IgG(2

85 omparable to those of mammalian TCR in basic paratope structure; additionally, nurse shark TCRdelta C

86 The paratope surface consists of residues located in four co

87 nfirmed that the mutated residue retains the paratope surface when compared with WT PG9.

88 yranosonic acid), displays a germ-line-coded paratope that differs significantly from previously char

89 Comparison of the respective paratopes that bind to carbohydrate and protein reveals

90 ey are significantly less common among those paratopes that bind to the immunodominant amino-terminal

91 the context of lipids, shaping MPER-specific paratopes through selective pressure.

92 odify the V region structure to alter the Ab paratope, thus providing an explanation for how isotype

93 Six distinct paratope topologies observed for a single germline mAb p

94 y crystallography has shown that an antibody paratope typically binds 15-22 amino acids (aa) of an ep

95 Interestingly, the paratope was mapped exclusively to the variable light ch

96 the parent 10E8 was the most soluble, with a paratope we showed crystallographically to be virtually

97 structures of large protein Ag epitopes and paratopes were analyzed to inform the process of eliciti

98 The IgE and IgA paratopes were probed by nuclear magnetic resonance spec

99 The predicted functional paratopes were reasonably validated by the hot spot resi

100 ecifically to a distinct conformation of the paratope, which was also different from that of the Ag-f

101 hich conformational convergence of different paratopes while binding to a common epitope in a similar

102 novel approach to the problem by probing the paratope with (15)N label peptide mimetics followed by N

103 nal residues located at the periphery of the paratope with a concomitant loss of the so-called "O-rin

104 t a limited repertoire of antibodies bearing paratopes with diverse structural contours enriched with

105 Engineered antibody paratopes with limited sequence diversity permit assessm

106 methods were used to predict the functional paratopes with the 3D antibody variable domain structure

107 hain V region gene products to form specific paratopes, with no apparent tendency for conservation of

108 e the major part of the predicted functional paratopes, with short-chain hydrophilic residues forming