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 | Family |
| Description | Cathelicidins are antimicrobial peptides and, together with defensins, form a large group of cationic peptides with amphipathic properties, and are part of the innate immune system in many vertebrates. These peptides exert antimicrobial activity against a wide range of microorganisms such as bacteria, enveloped viruses and fungi. They were first described in bone marrow myeloid cells from mammals but they are also present in several organisms, as antimicrobial peptides are a conserved immune response in all organisms [, ].Structurally, these proteins consist of a highly conserved N-terminal "cathelin' domain including a signal sequence and a conserved region of about 100 residues that contains four cysteines involved in two disulphide bonds, and a highly divergent C-terminal section of variable size [ ]. It is in this C-terminal section that the antibacterial peptides are found; they are proteolytically processed from their precursor by enzymes such as elastase. This structure is shown in the following schematic representation:+---+--------------------------------+--------------------+ |Sig| Propeptide C C C C | Antibacterial pep. |+---+----------------|--|--|--|------+--------------------+ | | | |+--+ +--+ 'C': conserved cysteine involved in a disulphide bond.Cathelicidins-related peptides from reptiles are also included in this family. They are potent antimicrobial peptides with low cytotoxicity, being interesting candidates as antimicrobial agents [ ]. |
| Short Name | Cathelicidin-like |
