| Primary Identifier | IPR000034 | Type | Domain |
| Short Name | Laminin_IV |
| description | Laminin is a large molecular weight glycoprotein present only in basementmembranes in almost every animal tissue. Each laminin is a heterotrimerassembled from alpha, beta and gamma chain subunits, secreted and incorporatedinto cell-associated extracellular matrices. The laminins can self-assemble,bind to other matrix macromolecules, and have unique and shared cellinteractions mediated by integrins, dystroglycan, and other receptors. Throughthese interactions, laminins critically contribute to cell differentiation,shape and movement, maintenance of tissue phenotypes,and promotion of tissuesurvival [, ].The different laminin chains share a 600-residue domain I/II whicholigomerises into a rod-like coiled-coil structure forming the long arm oflaminins. The N-terminal short arms consist of rod-like elements (domain IIIand V) formed by tandem arrays of laminin-type EGF modulesand several globular domains: domains IV and domain VI (lamininN-terminal). All alpha chains share a unique C-terminal Gdomain which consists of five laminin G modules []. Laminin IV domain is also found in the perlecan protein, an integral component ofbasement membranes, which serves also as an attachment substrate for cells,but it is not found in short laminin chains (alpha4 or beta3). The function ofthis domain is not yet known. |
