Tuba
From Proteopedia
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| - | <StructureSection load='4cc2' size='340' side='right' caption='Human Tuba 6th SH3 domain complex with N-WASP peptide, glycerol and Cl- ion (PDB code [[4cc2]])' scene=''> | + | <StructureSection load='4cc2' size='340' side='right' caption='Human Tuba 6th SH3 domain (grey) complex with N-WASP peptide (green), glycerol and Cl- ion (PDB code [[4cc2]])' scene=''> |
== Function == | == Function == | ||
'''Tuba''' or '''dynamin-binding protein''' is a scaffold protein found in brain synapses which brings together dynamin and actin regulatory proteins. The N-terminal SH3 domains bind dynamin and the C-terminal SH3 domain binds actin regulatory proteins<ref>PMID:14506234</ref>. | '''Tuba''' or '''dynamin-binding protein''' is a scaffold protein found in brain synapses which brings together dynamin and actin regulatory proteins. The N-terminal SH3 domains bind dynamin and the C-terminal SH3 domain binds actin regulatory proteins<ref>PMID:14506234</ref>. | ||
| + | For more details see [[Schubert lab: bacterial InIC disrupts human Tuba complexes]]. | ||
== Disease == | == Disease == | ||
Tuba deficiency causes and abnormal renal ciliary and morphogenetic phenotype. Tuba has a critical role in ciliogenesis and nephrogenesis by regulating Cdc42 activity<ref>PMID:26895965</ref>. | Tuba deficiency causes and abnormal renal ciliary and morphogenetic phenotype. Tuba has a critical role in ciliogenesis and nephrogenesis by regulating Cdc42 activity<ref>PMID:26895965</ref>. | ||
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| - | == Relevance == | ||
== Structural highlights == | == Structural highlights == | ||
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Tuba contains 6 SH3 domains. The C-terminal 6th SH3 domain binds proline-rich regions of human actin regulating proteins such as N-WASP and Mena. The peptide forms a polyproline type II helix. The interactions of Tuba with the peptide is via SH3-conserved residues<ref>PMID:24332715</ref>. | Tuba contains 6 SH3 domains. The C-terminal 6th SH3 domain binds proline-rich regions of human actin regulating proteins such as N-WASP and Mena. The peptide forms a polyproline type II helix. The interactions of Tuba with the peptide is via SH3-conserved residues<ref>PMID:24332715</ref>. | ||
| - | + | ==Tuba 3D structures== | |
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| + | See [[Tuba 3D structures]] | ||
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== References == | == References == | ||
<references/> | <references/> | ||
| + | [[Category:Topic Page]] | ||
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