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We are deeply saddened by the passing of Amos Bairoch (1957–2025), the creator of PROSITE. We wish to dedicate our latest paper, published shortly before his death, to him. He will always be a source of inspiration to us.
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Amos Bairoch

PROSITE documentation PDOC50927
Bulb-type lectin domain profile


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PURL: https://purl.expasy.org/prosite/documentation/PDOC50927

Description

A bulb lectin super-family (Amaryllidaceae, Orchidaceae and Aliaceae) contains a ~115-residue-long domain whose overall three dimensional fold is very similar to that of [1,2]:

  • Dictyostelium discoideum comitin, an actin binding protein,
  • Curculigo latifolia curculin, a sweet tasting and taste-modifying protein.

Although this domain is a mannose-binding lectin in the bulb super-family, curculin is considered as a non-functional mannose-binding protein devoid of mannose-binding activity [1].

Each bulb-type lectin domain consists of three sequential β-sheet subdomains (I, II, III) that are inter-related by pseudo three-fold symmetry (see <PDB:1MSA>). The three subdomains are flat four-stranded, antiparrallel β-sheets. Together they form a 12-stranded β-barrel in which the barrel axis coincides with the pseudo 3-fold axis [2].

The profile we developed covers the entire bulb-type lectin domain.

Last update:

September 2003 / First entry.

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Technical section

PROSITE method (with tools and information) covered by this documentation:

BULB_LECTIN, PS50927; Bulb-type lectin domain profile  (MATRIX)


References

1AuthorsBarre A. Van Damme E.J.M. Peumans W.J. Rouge P.
TitleCurculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin.
SourcePlant Mol. Biol. 33:691-698(1997).
PubMed ID9132060

2AuthorsHester G. Kaku H. Goldstein I.J. Wright C.S.
TitleStructure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family.
SourceNat. Struct. Biol. 2:472-479(1995).
PubMed ID7664110



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