Tau protein: Difference between revisions
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==Structure and Function == | ==Structure and Function == | ||
The human '''tau protein''', encoded by chromosome 17q21, has a natively unfolded protein structure, which contributes to its flexibility and ability to stabilize functional microtubules <ref name="mandelkow">PMID: 22762014</ref>. Specifically, its primary structure, consisting of <scene name='71/716561/Primary_tau/1'>serines, threonines, aspartates, glutamates, lysines, arginines, prolines, and aromatics</scene>, is highly hydrophilic compared to other cytosolic proteins <ref name="mandelkow"/>. It has a predominantly acidic N-terminal region, a proline-rich middle region, and a relatively neutral C-terminal region <ref name="mandelkow"/>. | The human '''tau protein''' or '''microtubule-associated protein tau''', encoded by chromosome 17q21, has a natively unfolded protein structure, which contributes to its flexibility and ability to stabilize functional microtubules <ref name="mandelkow">PMID: 22762014</ref>. Specifically, its primary structure, consisting of <scene name='71/716561/Primary_tau/1'>serines, threonines, aspartates, glutamates, lysines, arginines, prolines, and aromatics</scene>, is highly hydrophilic compared to other cytosolic proteins <ref name="mandelkow"/>. It has a predominantly acidic N-terminal region, a proline-rich middle region, and a relatively neutral C-terminal region <ref name="mandelkow"/>. | ||
Additionally, tau has a transient secondary structure of α-helices, β-pleated sheets, and a poly-proline II helix <ref name="mandelkow"/>. Tau does not resemble a globular protein, but has characteristics of a denatured, unfolded protein which contributes to its overall hydrophilicity <ref name="schweers">PMID: 7929085</ref>. It can also interact with other tau proteins to form <scene name='71/716561/Tau_aggregation/1'>aggregations</scene>. | Additionally, tau has a transient secondary structure of α-helices, β-pleated sheets, and a poly-proline II helix <ref name="mandelkow"/>. Tau does not resemble a globular protein, but has characteristics of a denatured, unfolded protein which contributes to its overall hydrophilicity <ref name="schweers">PMID: 7929085</ref>. It can also interact with other tau proteins to form <scene name='71/716561/Tau_aggregation/1'>aggregations</scene>. | ||
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'''Parkinson’s Disease''' | '''Parkinson’s Disease''' | ||
Protein aggregation also exists in patients suffering from Parkinson’s disease, specifically within the substantia nigra of the midbrain <ref name="Ross">PMID: 15272267</ref>. Immunohistochemical studies reveal that abnormally phosphorylated tau proteins are partially involved in the development of Lewy bodies, protein aggregates, within the substantia nigra <ref name="Ishizawa">PMID: 12722831</ref>. Lewy bodies may be involved in the neurodegeneration of dopaminergic neurons within this area <ref name="Ross"/>. | Protein aggregation also exists in patients suffering from Parkinson’s disease, specifically within the substantia nigra of the midbrain <ref name="Ross">PMID: 15272267</ref>. Immunohistochemical studies reveal that abnormally phosphorylated tau proteins are partially involved in the development of Lewy bodies, protein aggregates, within the substantia nigra <ref name="Ishizawa">PMID: 12722831</ref>. Lewy bodies may be involved in the neurodegeneration of dopaminergic neurons within this area <ref name="Ross"/>. | ||
==3D Structures of tau protein== | |||
</StructureSection> | </StructureSection> | ||
==3D Structures of tau protein== | ==3D Structures of tau protein== | ||
[[Tau protein 3D structures]] | |||
Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | Updated on {{REVISIONDAY2}}-{{MONTHNAME|{{REVISIONMONTH}}}}-{{REVISIONYEAR}} | ||