Fascin Conclusion: Difference between revisions
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Through the creation of Phylogency trees, it was found that fascin 1 was is a protein specific to Eukaryotic organisms. Fascin evolution occured early as it was found within the Animalia kingdom. Even subkingdoms of Animalia were found to have fascin 1 protein and thus it can be determined that Fascin 1 could be first identified with then first Eukaryotic organisms. However due to Fascin 1 not being found with other orders of life, the protein was formed after the Last Common Ancestor. | Through the creation of Phylogency trees, it was found that fascin 1 was is a protein specific to Eukaryotic organisms. Fascin evolution occured early as it was found within the Animalia kingdom. Even subkingdoms of Animalia were found to have fascin 1 protein and thus it can be determined that Fascin 1 could be first identified with then first Eukaryotic organisms. However due to Fascin 1 not being found with other orders of life, the protein was formed after the Last Common Ancestor. | ||
Structurally little is known about the binding of Fascin to its target molecule actin. An attempt was made to deduce this site through amalgamation of binding pocket analysis, residue conservation, electrostatic surface analysis and through currently known research (of which there is fairly little). The proposed binding sites are localised to residues 136-143 and 386-395 on both subgroups (they are the same molecule back to back). Other important sites include Ser39 which is the PKC phosphorylation site used for activation/deactivation of actin binding function. | Structurally little is known about the binding of Fascin to its target molecule actin. An attempt was made to deduce this site through amalgamation of binding pocket analysis, residue conservation, electrostatic surface analysis and through currently known research (of which there is fairly little). The proposed binding sites are localised to residues 136-143 and 386-395 on both subgroups (they are the same molecule back to back). Other important sites include Ser39 which is the PKC phosphorylation site used for activation/deactivation of actin binding function (Ono S et.al. 1997) | ||
The back to back subgroup model fits well with the action of Fascin as it's actin crossbundling function means it must bind two actin molecules at diametrically opposing ends of itself. ( | The back to back subgroup model fits well with the action of Fascin as it's actin crossbundling function means it must bind two actin molecules at diametrically opposing ends of itself. (Aratyn Y et.al. 2007) | ||
[[Fascin Abstract | Abstract]] | [[Fascin Introduction | Introduction]] | [[Fascin Methods | Methods]] | [[Fascin Results | Results]] | [[Fascin Discussion | Discussion]] | [[Fascin Conclusion | Conclusion]] | [[Fascin Appendix | Appendix]] | [[Fascin References | References]] | [[Fascin Abstract | Abstract]] | [[Fascin Introduction | Introduction]] | [[Fascin Methods | Methods]] | [[Fascin Results | Results]] | [[Fascin Discussion | Discussion]] | [[Fascin Conclusion | Conclusion]] | [[Fascin Appendix | Appendix]] | [[Fascin References | References]] | ||
<br>[[Fascin 1 | Back to main page]] | <br>[[Fascin 1 | Back to main page]] | ||
Revision as of 00:38, 16 June 2009
Conclusion
Through the creation of Phylogency trees, it was found that fascin 1 was is a protein specific to Eukaryotic organisms. Fascin evolution occured early as it was found within the Animalia kingdom. Even subkingdoms of Animalia were found to have fascin 1 protein and thus it can be determined that Fascin 1 could be first identified with then first Eukaryotic organisms. However due to Fascin 1 not being found with other orders of life, the protein was formed after the Last Common Ancestor.
Structurally little is known about the binding of Fascin to its target molecule actin. An attempt was made to deduce this site through amalgamation of binding pocket analysis, residue conservation, electrostatic surface analysis and through currently known research (of which there is fairly little). The proposed binding sites are localised to residues 136-143 and 386-395 on both subgroups (they are the same molecule back to back). Other important sites include Ser39 which is the PKC phosphorylation site used for activation/deactivation of actin binding function (Ono S et.al. 1997)
The back to back subgroup model fits well with the action of Fascin as it's actin crossbundling function means it must bind two actin molecules at diametrically opposing ends of itself. (Aratyn Y et.al. 2007)
Abstract | Introduction | Methods | Results | Discussion | Conclusion | Appendix | References
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