{PDOC50927}
{PS50927; BULB_LECTIN}
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* Bulb-type lectin domain profile *
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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  beta-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
beta-sheets. Together  they form a 12-stranded beta-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.

-Sequences known to belong to this class detected by the profile: ALL.
-Other sequence(s) detected in Swiss-Prot: NONE.
-Last update: September 2003 / First entry.

[ 1] Barre A., Van Damme E.J.M., Peumans W.J., Rouge P.
     "Curculin, a sweet-tasting and taste-modifying protein, is a
     non-functional mannose-binding lectin."
     Plant Mol. Biol. 33:691-698(1997).
     PubMed=9132060
[ 2] Hester G., Kaku H., Goldstein I.J., Wright C.S.
     "Structure of mannose-specific snowdrop (Galanthus nivalis) lectin is
     representative of a new plant lectin family."
     Nat. Struct. Biol. 2:472-479(1995).
     PubMed=7664110

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