LIS - Legume Information System
Information about legume traits for crop improvement
CicerMine
v5.1.0.3
Cicer data from the Legume Information System
v5.1.0.3
Cicer data from the Legume Information System
| Type | Conserved_site |
| Description | The seeds of cereals contain numerous serine protease and alpha-amylase inhibitors. These inhibitors can be grouped into families based on structural similarities. This domain identifies sequences belonging to the cereal (monocotyledon) trypsin/alpha-amylase inhibitor family [ ]. It includes those annotated solely as seed allergens or alpha-amyalse inhibitors []. Many belong to MEROPS inhibitor family I6, clan IJ. Some are known to be inhibit trypsin (an S1 peptidase, ) [ ]. For some there is no direct evidence to suggest they any can inhibit trypsin or any other serine peptidase. Studies on the alpha-amylase inhibitor from Secale cereale (Rye) has demonstrated no activity against trypsin, and illustrates the necessity of exercising caution in assigning function based on sequence comparisons [ ]. The cereal trypsin/alpha-amylase inhibitor family consists of proteins of about 120 amino acids which contain 10 cysteine residues, all of which are involved in disulphide bonds [ ]. The schematic representation of the structure of these inhibitors is shown below:+----------------------------+ +----------+| +-+ || || | | | xxCxxxxxxCxxxCxxxxxxCCxxxCxCxxxxxxxxxxxxxCxxxxxxxxCxxxxxxxCxxxx| | | | | +---------------------------+ |+-------------------------------------------------------+ 'C': conserved cysteine involved in a disulphide bond.The 3D structure of the bifunctional alpha-amylase/trypsin inhibitor (RBI) from seeds of Eleusine coracana (Indian finger millet) has been determined in solution using multidimensional 1H and 15N NMR spectroscopy [ ]. The inhibitor forms a globular 4-helix motif with a simple 'up-and-down' topology, and includes a short anti-parallel β-sheet []. |
| Short Name | Allergen/tryp_amyl_inhib_CS |
