Concanavalin

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Function

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.[1].

  • Concanavalin B (ConB) is related to chitinase with 40% sequence identity.[2].
  • Concanavalin BR (ConBR) is ConA from Brazilian jack bean.
  • Concanavalin V (ConV) is a D-mannose/D-glucose-binding lectin.

Relevance

ConA has therapeutic effect on liver cancer.

Structural highlights

ConA is the with D2 symmetry. ConA contains a as well as a .

3D Structures of Concanavalin

Concanavalin 3D structures


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

Drag the structure with the mouse to rotate

ReferencesReferences

  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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