Sandbox Reserved 779: Difference between revisions
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<big>'''β-Lactoglobulin | <big>'''β-Lactoglobulin'''</big> | ||
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===Regulation of the activity=== | ===Regulation of the activity=== | ||
The acitivity of ERM proteins is caused by the association of different regions within the protein. | The acitivity of ERM proteins is caused by the association of different regions within the protein. | ||
The C-terminal tail domain contains an F-actin binding site in the last 30 residues. This domain also interacts with the FERM domain. The FERM-tail complex represents an inactive form of the protein in which membrane protein and active binding sites are masked.<ref> | The C-terminal tail domain contains an F-actin binding site in the last 30 residues. This domain also interacts with the FERM domain. The FERM-tail complex represents an inactive form of the protein in which membrane protein and active binding sites are masked.<ref>doi: 10.1074/jbc.274.1.170</ref> | ||
The ERM proteins are regulated by changing from a close to an open conformation. This is due to severing of intramolecular head–tail interactions,and also of interactions between their FERM domain and α-helical domains<ref name="utile2">PMID:22012890</ref>.Conformational changes activate the proteins because they modify the intramolecular contacts, allowing them to bind to their partners. The FERM domain has a fundamental role because it allows ERM proteins to interact with integral proteins of the plasma membrane<ref>PMID:12154370</ref>. | The ERM proteins are regulated by changing from a close to an open conformation. This is due to severing of intramolecular head–tail interactions,and also of interactions between their FERM domain and α-helical domains<ref name="utile2">PMID:22012890</ref>.Conformational changes activate the proteins because they modify the intramolecular contacts, allowing them to bind to their partners. The FERM domain has a fundamental role because it allows ERM proteins to interact with integral proteins of the plasma membrane<ref>PMID:12154370</ref>. | ||
