| Description | Beta 1,3-glucan recognition proteins (GRP, also called Gram-negative bacteria binding proteins or GNBPs) have specific affinity for beta 1,3-glucan, a component on the surface of fungi and bacteria. Beta-GRP (beta-1,3-glucan recognition protein) is one of several pattern recognition receptors (PRRs), also referred to as biosensor proteins, that complexes with pathogen-associated beta-1,3-glucans and then transduces signals necessary for activation of an appropriate innate immune response. They are present in insects and lack all catalytic residues [ , , , , ].BGRP consists of a well conserved N-terminal domain and a C-terminal beta-1,3-glucanase-like domain [ , ]. The N-terminal domain of BGRP plays a critical role for the detection of pathogen. In contrast, the C-terminal glucanase-like domain has neither glucanase activity, nor affinity with the beta-1,3-glucan [, ].This superfamily represents a domain is found at the N terminus of beta-1,3-glucan-binding proteins (BGRP-N). Structurally, BGRP-N has an immunoglobulin-like β-sandwich fold composed of two antiparallel β-sheets containing three and five β-strands [ ]. | Name | Beta-1,3-glucan-binding protein, N-terminal domain superfamily |
| Short Name | BGBP_N_sf | Type | Homologous_superfamily |
Powered by
Have you tried our InterMine mobile apps?
and interoperation is funded by 
