novadock molecular docking tool Search Results


β turn mediate protein protein interactions  (DNASTAR)
93
DNASTAR β turn mediate protein protein interactions
(A) NovaDock predicted that Ank5 residues in AR3 and AR4 bind NLRC5. Presented are the amino acid sequences of AR3 and AR4 aligned with the consensus sequence for a eukaryotic AR and a schematic for AR secondary structure. Residues highlighted yellow (AR3 L68 and Y69; AR4 Y103 and S105) occur at positions 2, 3, and/or 5 in <t>the</t> <t>β-turn</t> that tend to mediate protein-protein interactions. Those highlighted cyan are at positions in the inner α-helix that would alter AR tertiary structure if mutated. (B) Novadock modeled interaction between Ank5 and NLRC5. The secondary structures of Ank5 AR3 and AR4 are red while that of the NLRC5 NACHT domain is green. The Ank5 residues predicted to interact with NLRC5 and that were targeted for alanine substitution are labeled.
β Turn Mediate Protein Protein Interactions, supplied by DNASTAR, used in various techniques. Bioz Stars score: 93/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
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β turn mediate protein protein interactions - by Bioz Stars, 2026-07
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protean 3d version 17 4 3 2  (DNASTAR)
95
DNASTAR protean 3d version 17 4 3 2
(A) NovaDock predicted that Ank5 residues in AR3 and AR4 bind NLRC5. Presented are the amino acid sequences of AR3 and AR4 aligned with the consensus sequence for a eukaryotic AR and a schematic for AR secondary structure. Residues highlighted yellow (AR3 L68 and Y69; AR4 Y103 and S105) occur at positions 2, 3, and/or 5 in <t>the</t> <t>β-turn</t> that tend to mediate protein-protein interactions. Those highlighted cyan are at positions in the inner α-helix that would alter AR tertiary structure if mutated. (B) Novadock modeled interaction between Ank5 and NLRC5. The secondary structures of Ank5 AR3 and AR4 are red while that of the NLRC5 NACHT domain is green. The Ank5 residues predicted to interact with NLRC5 and that were targeted for alanine substitution are labeled.
Protean 3d Version 17 4 3 2, supplied by DNASTAR, used in various techniques. Bioz Stars score: 95/100, based on 1 PubMed citations. ZERO BIAS - scores, article reviews, protocol conditions and more
https://www.bioz.com/product/novadock+molecular+docking+tool/bio_rxiv__2025__10__02__679962-227-13-17?v=DNASTAR
Average 95 stars, based on 1 article reviews
protean 3d version 17 4 3 2 - by Bioz Stars, 2026-07
95/100 stars
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Image Search Results


(A) NovaDock predicted that Ank5 residues in AR3 and AR4 bind NLRC5. Presented are the amino acid sequences of AR3 and AR4 aligned with the consensus sequence for a eukaryotic AR and a schematic for AR secondary structure. Residues highlighted yellow (AR3 L68 and Y69; AR4 Y103 and S105) occur at positions 2, 3, and/or 5 in the β-turn that tend to mediate protein-protein interactions. Those highlighted cyan are at positions in the inner α-helix that would alter AR tertiary structure if mutated. (B) Novadock modeled interaction between Ank5 and NLRC5. The secondary structures of Ank5 AR3 and AR4 are red while that of the NLRC5 NACHT domain is green. The Ank5 residues predicted to interact with NLRC5 and that were targeted for alanine substitution are labeled.

Journal: bioRxiv

Article Title: Orientia tsutsugamushi Ank5 directs ubiquitination and proteasomal degradation of NLRC5 to inhibit major histocompatibility complex class I expression

doi: 10.1101/2023.12.04.569938

Figure Lengend Snippet: (A) NovaDock predicted that Ank5 residues in AR3 and AR4 bind NLRC5. Presented are the amino acid sequences of AR3 and AR4 aligned with the consensus sequence for a eukaryotic AR and a schematic for AR secondary structure. Residues highlighted yellow (AR3 L68 and Y69; AR4 Y103 and S105) occur at positions 2, 3, and/or 5 in the β-turn that tend to mediate protein-protein interactions. Those highlighted cyan are at positions in the inner α-helix that would alter AR tertiary structure if mutated. (B) Novadock modeled interaction between Ank5 and NLRC5. The secondary structures of Ank5 AR3 and AR4 are red while that of the NLRC5 NACHT domain is green. The Ank5 residues predicted to interact with NLRC5 and that were targeted for alanine substitution are labeled.

Article Snippet: Within this region, conserved residues preserve tertiary structure while non-conserved or semi-conserved residues at positions 2, 3, and 5 in the β-turn mediate protein-protein interactions and dictate target specificity., , In agreement with pulldown studies ( and ), NovaDock predicted that Ank5 AR3 and AR4 bind NLRC5.

Techniques: Sequencing, Labeling