Neuraminidase

From Proteopedia

Revision as of 08:47, 22 August 2017

spinqualitylabelsall models H5N1 avian influenza virus neuraminidase complex with Tamiflu (PDB entry 2ht7) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image Contents 1 Function 2 Relevance 3 Structural highlights Function Neuraminidase (NAN) cleaves the glycosidic bonds of neuraminic acid[1]. endo-neuraminidase is a phage neuraminidase which cleaves α-2,8-polysialic acid[2]. Pseudaminidase is a Pseudomonas aeruginosa neuraminidase. Trans-sialidase transfers sialic acid from Trypanosoma cruzi to a host cell[3]. See also Avian Influenza Neuraminidase, Tamiflu and Relenza Zanamivir (Relenza) Molecular Playground/Relenza Molecular Playground/Tamiflu Oseltamivir (Tamiflu) Treatments:Influenza User:Michael Strong/H1N1/NA for Influenza virus neuraminidase User:Michael Strong/H1N1/NA/MSA for multiple sequence alignment. For other inhibitors see Neuraminidase Inhibitor Pharmacokinetics Carbohydrate binding domain from Streptococcus pneumoniae NanA sialidase complexed with 3'-sialyllactose Treatments:Neuraminidase Inhibitor Pharmacokinetics References . Relevance The viral NAN is a drug target for prevention of influenza[4]. In Chagas disease trans-sialidase on the surface of Trypanosoma cruzi participate in host-parasite interactions and mediate the initial stages of the invasion of the host cell[5]. Structural highlights The biological assembly of H5N1 avian influenza virus neuraminidase is . The [6].

3D structures of Neuraminidase

Updated on 22-August-2017 {{#tree:id=OrganizedByTopic|openlevels=0|

• Neuraminidase

• • 2ya4, 2w20, 2vvz – SpNANA catalytic domain – Streptococcus pneumoniae
    
  • 3h71 - SpNANA catalytic domain precursor
    
  • 4zxk - SpNANA carbohydrate-binding domain
    
  • 2vw0, 2vw1, 2vw2 - SpNANB
    
  • 4xmi, 4xma, 4xjz, 4xj8, 4xio, 4xik – SpNANB (mutant)
    
  • [[4yz4, 4yw4 – SpNANC
    
  • 2xzi, 2xzj, 2xzk, 2xcy – NANA – Aspergillus fumigatus
    
  • 2w68 – VcNANA sialic acid binding domain – Vibrio cholerae
    
  • 1w0o, 1kit– VcNANA
    
  • 1snt, 1so7 – hNeu2 - human
    
  • 2f24, 2f26, 2f28 – hNeu2 (mutant)
    
  • 1eur - MvNANA residues 43-407 – Micromonospora viridifaciens
    
  • 1euu - MvNANA residues 47-647
    
  • 1wcq, 1w8n, 1w8o, 2hu0, 2hu4 – MvNANA residues 47-647 (mutant)
    
  • 3sil – StNANA (mutant) – Salmonella typhimurium
    
  • 4bbw, 5muk – BtNAN – Bacterioides thetaiotaomicron
    

• Binary complexes of Neuraminidase

• • 3h72 - SpNANA catalytic domain precursor + sialic derivative
    
  • 3h73 - SpNANA catalytic domain precursor + sialic acid analog
    
  • 2ya5 - SpNANA catalytic domain + sialic acid
    
  • 2ya7, 2ya8, 5kky, 5f9t - SpNANA catalytic domain + inhibitor
    
  • 2ya6 - SpNANA catalytic domain + sialic acid analog
    
  • 2jkb - SpNANB residues 30-697 + sialic acid analog
    
  • 4c1w - SpNANB residues 52-236 + sialic acid derivative
    
  • 4foq, 4fov, 4fow, 4foy, 4fp2, 4fp3, 4fpc, 4fpe, 4fpf, 4fpg, 4fph, 4fpj, 4fpk, 4fpl, 4fpo, 4fpy, 4fq4 – SpNANB + inhibitor
    
  • 4xyx – SpNANB + drug
    
  • 4xog, 4xjw, 4xj9, 4xil, 4xe9 – SpNANB (mutant) + drug
    
  • 4xju, 4xja, 4xhx, 4xhb – SpNANB (mutant) + inhibitor
    
  • 4yz2, 4yw3, 4wy2, 4wy1 – SpNANC + inhibitor
    
  • 4yz3, 4yw5 – SpNANC + drug
    
  • 1w0p – VcNANA + sialic derivative
    
  • 2f0z, 2f10, 2f11, 2f12, 2f13 – hNeu2 + inhibitor
    
  • 2f25, 2f27, 2f29, 4nc5, 4ncs - hNeu2 (mutant) + sialic acid analog
    
  • 1vcu - hNeu2 + sialic acid analog
    
  • 1eus - MvNANA residues 43-407 + neuraminic acid derivative
    
  • 2bzd - MvNANA residues 47-647 (mutant) + galactose
    
  • 1eut - MvNANA residues 47-647 + galactose
    
  • 5mul – BtNAN + glucuronic acid
    
  • 2ber - MvNANA residues 47-647 (mutant) + sialic derivative
    
  • 1dil, 1dim – StNANA + inhibitor
    
  • 2sim, 2sil - StNANA + neuraminic acid derivative
    

• Influenza virus neuraminidase

• • 3nss, 3k36, 3beq, 3cye, 2cml, 2b8h, 2ht5, 1v0z, 1nn2, 4hzv, 4fvk, 4gez – IvNANA residues 82-469 – Influenza virus
    
  • 4fvk, 4gez - IvNANA residues 76-442
    
  • 3k38, 4hzy – IvNANA (mutant)
    
  • 4gzo, 4k1h, 4k1i, 4k1k - IvNAN N2 residues 77-469
    
  • 4gzs, 4k1j - IvNAN N2 residues 77-469 (mutant)
    
  • 2ht5 – IvNAN N8 residues 82-469
    
  • 2htv - IvNAN N4 residues 82-469
    
  • 2hty - IvNAN N1 residues 82-469
    
  • 2qwa - IvNAN N9 Tern (mutant)
    
  • 4b7m - IvNAN H1n1
    
  • 4qn4 – IvNAN H3n6
    
  • 4wa3 – IvNAN H3n8
    
  • 5hug, 2ht5, 2htv, 2hty – IvNAN H5n1
    
  • 5huk – IvNAN H5n2
    
  • 5hun, 5hum – IvNAN H5n6
    
  • 5l14, 3nn9, 4nn9, 5nn9, 6nn9, 4mwj, 4mwl – IvNAN H7n9
    
  • 4qn3 – IvNAN H10n7
    
  • 7nn9 - IvNAN H11n9 Tern
    
  • 3sal - IvNAN H12n5 residues 82-469
    
  • 4gdi, 4gdj - IvNAN H17n10
    
  • 4mc7 – IvNAN H18n11
    

• Binary complexes of Influenza virus neuraminidase

• • 3o9j, 3o9k, 2c4a, 2c4l, 1w1x, 1w20, 1w21, 1nsb, 1nsc, 1nsd – IvNANA + sialic derivative
    
  • 3k37, 3b7e, 1vcj, 1l7f, 1f8c, 1f8d, 1f8e, 1a4g, 1a4q, 1b9t, 1b9v, 1b9s, 1inf, 1ing, 1inh, 1ivb, 1ivc, 1ivd, 1ive, 1ivf, 1ivg, 4d8s, 4ks1, 4ks2, 4ks3, 4ks4, 4ks5, 4m3m, 4mju, 4mjv – IvNANA + inhibitor
    
  • 3k39, 3k3a, 3ckz, 3cl0, 3cl2, 1l7g, 1l7h - IvNANA (mutant) + inhibitor
    
  • 1f8b, 1inv, 1inw, 1inx, 1iny, 4gb1 – IvNANA + sialic acid analog
    
  • 3ti3, 3ti4, 3ti5, 3ti6 – IvNAN H1n1 + inhibitor
    
  • 4b7j, 4b7n, 4b7q, 4b7r - IvNAN H1n1 + drug
    
  • 4qnp - IvNAN H1n1 + antibody
    
  • 3tia, 3tib, 3tic – IvNAN H2n2 + inhibitor
    
  • 2bat, 4gzw, 4gzx, 4gzq – IvNAN H3n2 + sialic acid
    
  • 4gzp, 4gzt - IvNAN H3n2 + drug
    
  • 4qn6 - IvNAN H3n6 + drug
    
  • 4wa5, 4wa4 - IvNAN H3n8 + drug
    
  • 2ht7, 2ht8, 2htq, 2htu – IvNAN H5n1 + inhibitor
    
  • 2htr, 2htw – IvNAN H5n1 + sialic acid analog
    
  • 5l15, 5l17, 5jyy, 4mwq, 4mwr, 4mwu, 4mwv, 4mww, 4mwx, 4mwy, 4mx0 - IvNAN H7n9 + drug
    
  • 5l18 - IvNAN H7n9 + sialic acid
    
  • 4mwq, 4mwr, 4mwu, 4mwv, 4mww, 4mwx, 4mwy, 4mx0 - IvNAN H7n9 + flu drug
    
  • 4qn7- IvNAN H10n7 + drug
    
  • 1nna, 1nnb - IvNAN H11n9 + neuraminic acid derivative
    
  • 4dgr - IvNAN H11n9 + benzoic acid derivative
    
  • 4weg - IvNAN H11n9 + sialic acid derivative
    
  • 1bji, 1nnc - IvNAN H11n9 Tern + sialic acid analog
    
  • 1xoe, 1xog, 3w09 - IvNAN H11n9 Tern + inhibitor
    
  • 4qn5 - IvNAN H12n5 + sialic acid
    
  • 3san, 3ti8 - IvNAN H12N5 + flu drug
    
  • 3san, 3ti8 - IvNAN N5 + flu drug
    
  • 4hzw, 4hzx - IvNAN N3 + flu drug
    
  • 4hzz, 4i00 - IvNAN N3 (mutant) + flu drug
    
  • 4h52, 4h53 – IvNAN N2 + inhibitor
    
  • 2qwb - IvNAN N9 Tern (mutant) + sialic derivative
    
  • 2qwc, 2qwd, 2qwe - IvNAN N9 Tern (mutant) + sialic acid analog
    
  • 1mwe - IvNAN N9 Tern + sialic acid
    
  • 2qwf, 2qwg, 2qwh, 2qwi, 2qwj, 2qwk - IvNAN N9 Tern (mutant) + inhibitor
    
  • 1nma, 1nmb, 1a14, 1nca, 1ncb, 1ncc, 1ncd, 2aep, 2aeq, 1nmc - IvNAN N9 Tern + antibody – mouse
    

• Endo-neuraminidase

• • 3gvf, 3gvk, 3gvj – ENANA (mutant) residues 246-910 – Enterobacteria phage K1F
    
  • 3gvl, 3ju4 – ENANA residues 246-910
    
  • 3gw6 – ENANA residues 790-1064
    

• Pseudaminidase

• • 2w38, 3h6j – PNANA – Pseudomonas aeruginosa

• Trans-sialidase

• • 2sli, 1sli, 3sli – lTS + inhibitor – leech
    
  • 1mr5, 1ms3, 1ms4 - TcTS (mutant) – Trypanosoma cruzi
    
  • 1ms0 - TcTS (mutant) + DANA + lactose
    
  • 1ms1, 1ms8 - TcTS (mutant) + DANA
    
  • 3b69 - TcTS (mutant) + NANA derivative
    
  • 1ms5 - TcTS (mutant) + Na-S-Gal
    
  • 1ms9, 3pjq - TcTS (mutant) + lactose
    
  • 1s0i - TcTS (mutant) + sialyl-lactose
    
  • 1s0j - TcTS (mutant) + MUNANA
    
  • 3opz - TcTS (mutant) + antibody
    
  • 2ah2 - TcTS (mutant) + difluorosialic acid
    

}}

References

1. ↑ Matrosovich MN, Matrosovich TY, Gray T, Roberts NA, Klenk HD. Neuraminidase is important for the initiation of influenza virus infection in human airway epithelium. J Virol. 2004 Nov;78(22):12665-7. PMID:15507653 doi:http://dx.doi.org/10.1128/JVI.78.22.12665-12667.2004
2. ↑ Rutishauser U, Watanabe M, Silver J, Troy FA, Vimr ER. Specific alteration of NCAM-mediated cell adhesion by an endoneuraminidase. J Cell Biol. 1985 Nov;101(5 Pt 1):1842-9. PMID:4055897
3. ↑ Colli W. Trans-sialidase: a unique enzyme activity discovered in the protozoan Trypanosoma cruzi. FASEB J. 1993 Oct;7(13):1257-64. PMID:8405811
4. ↑ Sylte MJ, Suarez DL. Influenza neuraminidase as a vaccine antigen. Curr Top Microbiol Immunol. 2009;333:227-41. doi: 10.1007/978-3-540-92165-3_12. PMID:19768409 doi:http://dx.doi.org/10.1007/978-3-540-92165-3_12
5. ↑ Schenkman S, Eichinger D, Pereira ME, Nussenzweig V. Structural and functional properties of Trypanosoma trans-sialidase. Annu Rev Microbiol. 1994;48:499-523. PMID:7826016 doi:http://dx.doi.org/10.1146/annurev.mi.48.100194.002435
6. ↑ Russell RJ, Haire LF, Stevens DJ, Collins PJ, Lin YP, Blackburn GM, Hay AJ, Gamblin SJ, Skehel JJ. The structure of H5N1 avian influenza neuraminidase suggests new opportunities for drug design. Nature. 2006 Sep 7;443(7107):45-9. Epub 2006 Aug 16. PMID:16915235 doi:http://dx.doi.org/10.1038/nature05114