Concanavalin

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m (Concanavalin A moved to Concanavalin: requested by Editor)
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== Function ==
== Function ==
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'''Concanavalin A''' (ConA) is a carbohydrate-binding protein from jack-bean (''Canavalia ensiformis''). It binds to certain sugars and to metal. It is used to characterize glycoproteins on cell surfaces.<ref>PMID:9546043</ref>. '''Concanavalin B''' (ConB) is related to chitinase with 40% sequence identity.<ref>PMID:7490746</ref>. '''Concanavalin V''' (ConV) is a D-mannose/D-glucose-binding lectin.
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'''Concanavalin A''' (ConA) is a carbohydrate-binding protein from jack-bean (''Canavalia ensiformis''). It binds to certain sugars and to metal. It is used to characterize glycoproteins on cell surfaces.<ref>PMID:9546043</ref>.
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*'''Concanavalin B''' (ConB) is related to chitinase with 40% sequence identity.<ref>PMID:7490746</ref>.
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*'''Concanavalin BR''' (ConBR) is ConA from Brazilian jack bean.
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*'''Concanavalin V''' (ConV) is a D-mannose/D-glucose-binding lectin.
== Relevance ==
== Relevance ==

Current revision

Concanavalin A complex with trisacchride, Mn+2 (small purple), Cl- (large green) and Ca+2 (small green) ions (large purple) (PDB entry 1qdc)

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References

  1. Loris R, Hamelryck T, Bouckaert J, Wyns L. Legume lectin structure. Biochim Biophys Acta. 1998 Mar 3;1383(1):9-36. PMID:9546043
  2. Hennig M, Jansonius JN, Terwisscha van Scheltinga AC, Dijkstra BW, Schlesier B. Crystal structure of concanavalin B at 1.65 A resolution. An "inactivated" chitinase from seeds of Canavalia ensiformis. J Mol Biol. 1995 Nov 24;254(2):237-46. PMID:7490746 doi:http://dx.doi.org/10.1006/jmbi.1995.0614

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Michal Harel, Alexander Berchansky, Eran Hodis, Jaime Prilusky

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