Spindlin: Difference between revisions
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<StructureSection load='4mzg' size='350' side='right' caption='Human spindlin-1 (skyblue) complex with histone H3 peptide (wheat) containing trimethyl lysine, MPD, Mg+2 (green) and Cl- (green) ions (PDB code [[4mzg]])' scene='77/778344/Cv/1'> | <StructureSection load='4mzg' size='350' side='right' caption='Human spindlin-1 (skyblue) complex with histone H3 peptide (wheat) containing trimethyl lysine, MPD, Mg+2 (green) and Cl- (green) ions (PDB code [[4mzg]])' scene='77/778344/Cv/1'> | ||
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== Function == | == Function == | ||
'''Spindlin-1''' (SPIN1) is a Tudor-like domain-containing protein is a histone methylation effector protein and facilitates the expression of rRNA genes<ref>PMID:21960006</ref>. SPIN1 senses a cis-tail histone H3 methylation pattern. | '''Spindlin-1''' (SPIN1) is a Tudor-like domain-containing protein which is a histone methylation effector protein and facilitates the expression of rRNA genes<ref>PMID:21960006</ref>. SPIN1 senses a cis-tail histone H3 methylation pattern. | ||
*'''Spindlin-2B''' is involved in the regulation of cell cycle progression. | *'''Spindlin-2B''' is involved in the regulation of cell cycle progression. | ||
*'''Spindlin-4''' binds trimethylated histone H3K4<ref>PMID:33636084</ref>. | |||
== Relevance == | == Relevance == | ||
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The crystal complex of SPIN1 and histone H3 peptide shows the <scene name='77/778344/Cv/4'>encapsulation of the histone trimethyllysine</scene> and <scene name='77/778344/Cv/5'>its Arg</scene> in hydrophobic pockets of SPIN1<ref>PMID:24589551</ref>. | The crystal complex of SPIN1 and histone H3 peptide shows the <scene name='77/778344/Cv/4'>encapsulation of the histone trimethyllysine</scene> and <scene name='77/778344/Cv/5'>its Arg</scene> in hydrophobic pockets of SPIN1<ref>PMID:24589551</ref>. | ||
== 3D Structures of spindlin == | == 3D Structures of spindlin == | ||
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== References == | == References == | ||
<references/> | <references/> | ||
</StructureSection> | |||
[[Category:Topic Page]] | [[Category:Topic Page]] |
Latest revision as of 10:42, 14 August 2024
FunctionSpindlin-1 (SPIN1) is a Tudor-like domain-containing protein which is a histone methylation effector protein and facilitates the expression of rRNA genes[1]. SPIN1 senses a cis-tail histone H3 methylation pattern.
RelevanceSPIN1 is implicated in liposarcoma and its inhibitors may represent a novel therapeutic strategy[3]. Structural highlightsThe crystal complex of SPIN1 and histone H3 peptide shows the and in hydrophobic pockets of SPIN1[4]. 3D Structures of spindlinUpdated on 29-May-2025 {{#tree:id=OrganizedByTopic|openlevels=0|
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