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InterPro: IPR001860 Glycoside hydrolase, family 34

Protein matchesHelp
UniProtKB
Matches:
13934 proteins
AccessionHelp IPR001860 Glyco_hydro_34
TypeHelp Family
SignaturesHelp
InterPro RelationshipsHelp
Contains IPR011040 Neuraminidase
GO Term annotationHelp
Process GO:0005975 carbohydrate metabolic process
Function GO:0004308 exo-alpha-sialidase activity
Component GO:0016020 membrane
InterPro annotation
BioMart Logo Entry Details in BioMart
AbstractHelp

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].

Structural linksHelp
PDB - click here
SCOP: b.68.1.1
CATH: 2.120.10.10
Database linksHelp
Enzyme: EC:3.2.1.18
CAZy: GH34
PANDIT: PF00064
Blocks: IPB001860

Taxonomic coverageHelp

Overlapping InterPro entriesHelp
IPR001860 Numbers of overlapping proteins Average numbers of overlapping amino acids

Example proteinsHelp
P03472 Neuraminidase

More proteins


Example Proteins Key


InterPro entry accession number/name and structure databases Colour code
IPR001860 Glycoside hydrolase, family 34
IPR011040 Neuraminidase
PDB Chain
ModBase
SCOP Domain
CATH Domain

PublicationsHelp
1. Henrissat B, Callebaut I, Fabrega S, Lehn P, Mornon JP, Davies G.
Conserved catalytic machinery and the prediction of a common fold for several families of glycosyl hydrolases.
Proc. Natl. Acad. Sci. U.S.A. 92 7090-4 1995 [PubMed: 7624375]
http://www.pubmedcentral.nih.gov/picrender.fcgi?tool=EBI&pubmedid=7624375&action=stream&blobtype=pdf
2. Davies G, Henrissat B.
Structures and mechanisms of glycosyl hydrolases.
Structure 3 853-9 1995 [PubMed: 8535779]
http://dx.doi.org/10.1016/S0969-2126(01)00220-9
3. Bairoch A.
Classification of glycosyl hydrolase families and index of glycosyl hydrolase entries in SWISS-PROT.
1999
4. Henrissat B, Coutinho PM.
Carbohydrate-Active Enzymes server.
1999
5. Couch RB.
Measures for control of influenza.
16 Suppl 1 41-5 1999 [PubMed: 10623375]

Additional ReadingHelp
Luo M.
Structural biology: antiviral drugs fit for a purpose.
Nature 443 2006 37-8 [PubMed: 16915238]
http://dx.doi.org/10.1038/nature05003
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
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
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
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