This domain family is found in bacteria, and is approximately 60 amino acids in length. The family is found in association with Pfam:PF00560, Pfam:PF08191, Pfam:PF09479. There are two completely conserved residues (I and F) that may be functionally i ...
This domain family is found in bacteria, and is approximately 60 amino acids in length. The family is found in association with Pfam:PF00560, Pfam:PF08191, Pfam:PF09479. There are two completely conserved residues (I and F) that may be functionally important. Internalin mediates bacterial adhesion and invasion of epithelial cells in the human intestine through specific interaction with its host cell receptor E-cadherin. This family is the N terminal of internalin, the cap domain of the protein. The cap domain is conserved between different internalin types. The cap domain does not interact with E cadherin, therefore its function is presumably structural: capping the hydrophobic core.
This is a GW domain found in the C-terminal of InlB proteins which belong to the extended family of internalin proteins found in Listeria [1]. These 80 residue GW domains are unique to InlB among the internalins but are present in other proteins of G ...
This is a GW domain found in the C-terminal of InlB proteins which belong to the extended family of internalin proteins found in Listeria [1]. These 80 residue GW domains are unique to InlB among the internalins but are present in other proteins of Gram-positive bacteria [2]. GW domains (named after a GlyTryp dipeptide) are structurally and evolutionary related to SH3 domains [1]. Despite of this, GW domains are unlikely to act as functional mimics of SH3 domains since their potential proline-binding sites are blocked or destroyed [2]. They are highly basic and interact with poly-anions. The GW domains are responsible for the non-covalent attachment to the bacterial cell surface through binding to lipoteichoic acid. The GW domains alone do not stimulate uptake, but they synergize with the Met-binding internalin domain [1].
