Home  |  Contact
PROSITE documentation PDOC50927 [for PROSITE entry PS50927]

Bulb-type lectin domain profile





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.

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



PROSITE is copyrighted by the SIB Swiss Institute of Bioinformatics and distributed under the Creative Commons Attribution-NonCommercial-NoDerivatives (CC BY-NC-ND 4.0) License, see prosite_license.html.

Miscellaneous

View entry in original PROSITE document format
View entry in raw text format (no links)