PROSITE documentation PDOC50927Bulb-type lectin domain profile
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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PROSITE method (with tools and information) covered by this documentation:
| 1 | Authors | Barre A. Van Damme E.J.M. Peumans W.J. Rouge P. |
| Title | Curculin, a sweet-tasting and taste-modifying protein, is a non-functional mannose-binding lectin. | |
| Source | Plant Mol. Biol. 33:691-698(1997). | |
| PubMed ID | 9132060 |
| 2 | Authors | Hester G. Kaku H. Goldstein I.J. Wright C.S. |
| Title | Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is representative of a new plant lectin family. | |
| Source | Nat. Struct. Biol. 2:472-479(1995). | |
| PubMed ID | 7664110 |
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