This entry represents a short domain found the matrilin (cartilage matrix) proteins. It forms a coiled coil structure and contains a single cysteine residue at its start which is likely to form a di-sulphide bridge with a corresponding cysteine in an upstream EGF domain, thereby spanning the VWA domain of the protein ( IPR002035 … expand

This entry represents a short domain found the matrilin (cartilage matrix) proteins. It forms a coiled coil structure and contains a single cysteine residue at its start which is likely to form a di-sulphide bridge with a corresponding cysteine in an upstream EGF domain, thereby spanning the VWA domain of the protein ( IPR002035 ). This domain is likely to be responsible for protein trimerisation [ PUBMED:9287130 PUBMED:9260286 ].

The Matrilin proteins are major components of the extracellular matrix, primarily found in cartilage. These proteins play a crucial role in the formation of extracellular filamentous networks and matrix assembly. Proteins such as Matrilin-1, Matrilin-2, Matrilin-3, and Matrilin-4 can form various oligomeric structures, including homooligomers and heterooligomers, which contribute to their functional diversity. They interact with other extracellular matrix proteins like COMP and collagen, facilitating the structural integrity and function of cartilage. Matrilin-1, also known as cartilage matrix protein, is specifically involved in non-articular cartilage and binds to collagen, further emphasising its role in maintaining cartilage structure [ PUBMED:24692560 ].