Sandbox bcce34
From Proteopedia
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==Focal Adhesion Kinase (FAK)== | ==Focal Adhesion Kinase (FAK)== | ||
<StructureSection load='2jkk' size='340' side='right' caption='FAK - Bis-Anilino Pyrimidine Inhibitor' scene=''> | <StructureSection load='2jkk' size='340' side='right' caption='FAK - Bis-Anilino Pyrimidine Inhibitor' scene=''> | ||
| - | This is a default text for your page '''Sandbox bcce34'''. Click above on '''edit this page''' to modify. Be careful with the < and > signs. | ||
| - | You may include any references to papers as in: the use of JSmol in Proteopedia <ref>DOI 10.1002/ijch.201300024</ref> or to the article describing Jmol <ref>PMID:21638687</ref> to the rescue. | ||
== Function == | == Function == | ||
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Focal adhesion kinase has four defined regions, or tertiary structure domains. Two of these domains, the N-terminal FERM domain and the Kinase domain form an auto-inhibitory interaction. This interaction is thought to be the result of hydrophobic interactions between the two domains and prevents the activation of the Kinase domain, FAK, thereby preventing the signalling function of FAK. Release of this auto-inhibitory interaction has been shown to occur within focal adhesions but not in the cytoplasm and therefore is thought to require interaction with focal adhesion proteins, potentially as a result of mechanical forces transmitted through the focal adhesion. | Focal adhesion kinase has four defined regions, or tertiary structure domains. Two of these domains, the N-terminal FERM domain and the Kinase domain form an auto-inhibitory interaction. This interaction is thought to be the result of hydrophobic interactions between the two domains and prevents the activation of the Kinase domain, FAK, thereby preventing the signalling function of FAK. Release of this auto-inhibitory interaction has been shown to occur within focal adhesions but not in the cytoplasm and therefore is thought to require interaction with focal adhesion proteins, potentially as a result of mechanical forces transmitted through the focal adhesion. | ||
| - | <scene name='59/596497/ | + | <scene name='59/596497/Fak_atp/1'>FAK - ATP</scene> |
| - | + | <scene name='59/596497/Ligand-receptor_complex/1'>Ligand - Receptor complex TAE226</scene> | |
| + | |||
| + | <scene name='59/596497/Ferm_domain/1'>FERM domain</scene> | ||
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| + | <scene name='59/596497/Ferm-kinase_domain/1'>FERM and Kinase domains</scene> | ||
| + | |||
| + | <scene name='59/596497/Ferm-kinase_domain-color/1'>FERM and Kinase domains colored</scene> | ||
| + | |||
| + | <scene name='59/596497/Fat_domain/1'>FAT domain</scene> | ||
</StructureSection> | </StructureSection> | ||
== References == | == References == | ||
<references/> | <references/> | ||
Current revision
Focal Adhesion Kinase (FAK)
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