1 Child Features
| DB identifier | Name | Short Name | Type |
|---|---|---|---|
| IPR018031 | Laminin B, subgroup | Laminin_B_subgr | Domain |
| Name | Laminin B type IV | Short Name | Laminin_B_type_IV |
| Type | Domain | Description | Laminins represent a distinct family of extracellular matrix proteins present only in basement membranes in almost every animal tissue. They are heterotrimeric molecules composed of alpha, beta and gamma subunits (formerly A, B1, and B2, respectively []) and form a cruciform structure consisting of 3 short arms, each formed by a different chain, and a long arm composed of all 3 chains, [, ]. Most of the globular domains of the short arms correspond to one of two different motifs, the 200-residue laminin N-terminal (domain VI) (LN) module and the 250-residue laminin domain IV (L4) module []. All alpha chains share a unique C-terminal G domain which consists of five laminin G modules. The laminins can self-assemble, bind to other matrix macromolecules, and have unique and shared cell interactions mediated by integrins, dystroglycan, and other receptors. There are at least 14 laminin isoforms that regulate a variety of cellular functions including cell adhesion, migration, proliferation, signalling and differentiation [, , ].The laminin B domain (also known as domain IV) is an extracellular module of unknown function. It is found in a number of different proteins that include, heparan sulphate proteoglycan from basement membrane, a laminin-like protein from Caenorhabditis elegansand laminin. Laminin IV domain is not found in short laminin chains (alpha4 or beta3). |
| DB identifier | Name | Short Name | Type |
|---|---|---|---|
| IPR018031 | Laminin B, subgroup | Laminin_B_subgr | Domain |
