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InterPro: IPR001860 Glycoside hydrolase, family 34
Protein matches
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UniProtKB Matches: 13934 proteins |
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Accession
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IPR001860 Glyco_hydro_34 |
Type
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Family |
Signatures
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InterPro Relationships
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Contains
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IPR011040 Neuraminidase
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GO Term annotation
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Process
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GO:0005975 carbohydrate metabolic process
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Function
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GO:0004308 exo-alpha-sialidase activity
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Component
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GO:0016020 membrane
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InterPro annotation
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Entry Details in BioMart
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Abstract
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O-Glycosyl hydrolases EC:3.2.1. are a widespread group of enzymes that hydrolyse the glycosidic bond between two or more carbohydrates, or between a carbohydrate and a non-carbohydrate moiety. A classification system for glycosyl hydrolases, based on sequence similarity, has led to the definition of 85 different families [1, 2, 3]. This classification is available on the CAZy (CArbohydrate-Active EnZymes) web site [4]. Because the fold of proteins is better conserved than their sequences, some of the families can be grouped in clans.
Glycoside hydrolase family 34 GH34 comprises enzymes with only one known activity; sialidase or neuraminidase EC:3.2.1.18.
Neuraminidases cleave the terminal sialic acid residues from carbohydrate chains in glycoproteins. Sialic acid is a negatively charged sugar associated with the protein and lipid portions of lipoproteins. In Influenza virus, neuraminidases prevent self-aggregation by removing the carbohydrate from the viral envelope thus facilitating the mobility of the virus to and from the site of infection.
Antiviral agents that inhibit influenza viral neuraminidase activity are of major importance in the control of influenza [5].
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Structural links
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Database links
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Additional Reading
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Luo M.
Structural biology: antiviral drugs fit for a purpose.
Nature 443 2006 37-8
[PubMed: 16915238]
http://dx.doi.org/10.1038/nature05003
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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 443 2006 45-9
[PubMed: 16915235]
http://dx.doi.org/10.1038/nature05114
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Smith BJ, Huyton T, Joosten RP, McKimm-Breschkin JL, Zhang JG, Luo CS, Lou MZ, Labrou NE, Garrett TP.
Structure of a calcium-deficient form of influenza virus neuraminidase: implications for substrate binding.
Acta Crystallogr. D Biol. Crystallogr. 62 2006 947-52
[PubMed: 16929094]
http://dx.doi.org/10.1107/S0907444906020063
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Venkatramani L, Bochkareva E, Lee JT, Gulati U, Graeme Laver W, Bochkarev A, Air GM.
An epidemiologically significant epitope of a 1998 human influenza virus neuraminidase forms a highly hydrated interface in the NA-antibody complex.
J. Mol. Biol. 356 2006 651-63
[PubMed: 16384583]
http://dx.doi.org/10.1016/j.jmb.2005.11.061
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Wang GT, Wang S, Gentles R, Sowin T, Maring CJ, Kempf DJ, Kati WM, Stoll V, Stewart KD, Laver G.
Design, synthesis, and structural analysis of inhibitors of influenza neuraminidase containing a 2,3-disubstituted tetrahydrofuran-5-carboxylic acid core.
Bioorg. Med. Chem. Lett. 15 2005 125-8
[PubMed: 15582424]
http://dx.doi.org/10.1016/j.bmcl.2004.10.022
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InterPro 23.1
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