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Literature summary for 3.4.21.91 extracted from

  • Yotmanee, P.; Rungrotmongkol, T.; Wichapong, K.; Choi, S.B.; Wahab, H.A.; Kungwan, N.; Hannongbua, S.
    Binding specificity of polypeptide substrates in NS2B/NS3pro serine protease of dengue virus type 2 A molecular dynamics study (2015), J. Mol. Graph. Model., 60, 24-33 .
    View publication on PubMed
Search for more literature for 3.4.21.91

Inhibitors

Inhibitors Comment Organism Structure
benzoyl-Nle-KRR homology model of the DV2 NS2B/NS3pro complexed with the peptidic inhibitor based on West nile virus structure Dengue virus type 2

Organism

Organism UniProt Comment Textmining
Dengue virus type 2 Q91H74 DENV-2
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Dengue virus type 2 Thailand/NGS-C/1944 Q91H74 DENV-2
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
additional information molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition Dengue virus type 2 ?
-
 ?
additional information molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition Dengue virus type 2 Thailand/NGS-C/1944 ?
-
 ?

Synonyms

Synonyms Comment Organism
DV2 NS2B/NS3pro
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 Dengue virus type 2
NS2B/NS3pro serine protease
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 Dengue virus type 2

General Information

General Information Comment Organism
additional information molecular dynamics simulations of the NS2B/NS3 protease complexes with six peptide substrates (capsid, intNS3, 2A/2B, 4B/5, 3/4A and 2B/3 containing the proteolytic site between P1 and P1' subsites) of DENV type 2 to compare the specificity of the protein-substrate binding recognition, overview. Although all substrates are in the active conformation for cleavage reaction by NS2B/NS3 protease, their binding strength is different. The simulated results of intermolecular hydrogen bonds and decomposition energies suggest that among the ten substrate residues (P5-P5') the P1 and P2 subsites play a major role in the binding with the focused protease. The arginine residue at these two subsites shows preferential binding at the active site. Besides, the P3, P1', P2' and P4' subsites show a less contribution in binding interaction. The catalytic water is detected nearby the carbonyl oxygen of the P1 reacting center of the capsid, intNS3, 2A/2B and 4B/5 peptides. The order of absolute binding free energy between these substrates and the NS2B/NS3 protease is capsid, intNS3, 2A/2B, 4B/5, 3/4A, 2B/3 in descending order in a relative correspondence with previous experimentally derived values. Hydrogen bond patterns of substrate binding Dengue virus type 2
physiological function the virus possesses a two-component (NS2B/NS3) serine protease that cleaves the viral precursor proteins Dengue virus type 2