Structure of the protein Laminin

Abstract

Abstract

Laminin is best described as a glycoprotein in which multiple protein domains are present. The role that laminins play in development, maintenance, and biological processes is extensive. The function of laminin, and all proteins, is dependent upon the structure of the protein. The domains of laminin can be described in terms of side chains, which consist of α5, β1, ϒ1 chains. The structure of laminin was difficult to determine due to the complexity of the protein. The use of many experimental techniques have been utilized in order to determine the molecular structure of laminin. These experimental techniques include small angle X-ray scattering (SAXS), analytical ultracentrifugation, dynamic light scattering, electron microscopy, and crystallization. Coupled together, these experimental results provide the most accurate prediction of what the structure of the protein laminin. With this experimentally determined structural representation, researchers can now begin looking into what the molecular mechanism for laminin polymerization actually is.