6mzd
From Proteopedia
(Difference between revisions)
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==Human TFIID Lobe A canonical== | ==Human TFIID Lobe A canonical== | ||
- | < | + | <SX load='6mzd' size='340' side='right' viewer='molstar' caption='[[6mzd]], [[Resolution|resolution]] 9.80Å' scene=''> |
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[6mzd]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MZD FirstGlance]. <br> | <table><tr><td colspan='2'>[[6mzd]] is a 12 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=6MZD OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=6MZD FirstGlance]. <br> | ||
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[[http://www.uniprot.org/uniprot/TBP_HUMAN TBP_HUMAN]] Defects in TBP are the cause of spinocerebellar ataxia type 17 (SCA17) [MIM:[http://omim.org/entry/607136 607136]]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA17 is an autosomal dominant cerebellar ataxia (ADCA) characterized by widespread cerebral and cerebellar atrophy, dementia and extrapyramidal signs. The molecular defect in SCA17 is the expansion of a CAG repeat in the coding region of TBP. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.<ref>PMID:11313753</ref> <ref>PMID:11448935</ref> <ref>PMID:11939898</ref> [[http://www.uniprot.org/uniprot/TAF1_HUMAN TAF1_HUMAN]] Defects in TAF1 are the cause of dystonia type 3 (DYT3) [MIM:[http://omim.org/entry/314250 314250]]; also called X-linked dystonia-parkinsonism (XDP). DYT3 is a X-linked dystonia-parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DYT3 is characterized by severe progressive torsion dystonia followed by parkinsonism. Its prevalence is high in the Philippines. DYT3 has a well-defined pathology of extensive neuronal loss and mosaic gliosis in the striatum (caudate nucleus and putamen) which appears to resemble that in Huntington disease.<ref>PMID:12928496</ref> <ref>PMID:17273961</ref> | [[http://www.uniprot.org/uniprot/TBP_HUMAN TBP_HUMAN]] Defects in TBP are the cause of spinocerebellar ataxia type 17 (SCA17) [MIM:[http://omim.org/entry/607136 607136]]. Spinocerebellar ataxia is a clinically and genetically heterogeneous group of cerebellar disorders. Patients show progressive incoordination of gait and often poor coordination of hands, speech and eye movements, due to degeneration of the cerebellum with variable involvement of the brainstem and spinal cord. SCA17 is an autosomal dominant cerebellar ataxia (ADCA) characterized by widespread cerebral and cerebellar atrophy, dementia and extrapyramidal signs. The molecular defect in SCA17 is the expansion of a CAG repeat in the coding region of TBP. Longer expansions result in earlier onset and more severe clinical manifestations of the disease.<ref>PMID:11313753</ref> <ref>PMID:11448935</ref> <ref>PMID:11939898</ref> [[http://www.uniprot.org/uniprot/TAF1_HUMAN TAF1_HUMAN]] Defects in TAF1 are the cause of dystonia type 3 (DYT3) [MIM:[http://omim.org/entry/314250 314250]]; also called X-linked dystonia-parkinsonism (XDP). DYT3 is a X-linked dystonia-parkinsonism disorder. Dystonia is defined by the presence of sustained involuntary muscle contractions, often leading to abnormal postures. DYT3 is characterized by severe progressive torsion dystonia followed by parkinsonism. Its prevalence is high in the Philippines. DYT3 has a well-defined pathology of extensive neuronal loss and mosaic gliosis in the striatum (caudate nucleus and putamen) which appears to resemble that in Huntington disease.<ref>PMID:12928496</ref> <ref>PMID:17273961</ref> | ||
== Function == | == Function == | ||
- | [[http://www.uniprot.org/uniprot/TBP_HUMAN TBP_HUMAN]] General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter. SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA.<ref>PMID:15970593</ref> [[http://www.uniprot.org/uniprot/ | + | [[http://www.uniprot.org/uniprot/TAF9_HUMAN TAF9_HUMAN]] Essential for cell viability. TAF9 and TAF9B are involved in transcriptional activation as well as repression of distinct but overlapping sets of genes. May have a role in gene regulation associated with apoptosis. TAFs are components of the transcription factor IID (TFIID) complex, the TBP-free TAFII complex (TFTC), the PCAF histone acetylase complex and the STAGA transcription coactivator-HAT complex. TFIID or TFTC are essential for the regulation of RNA polymerase II-mediated transcription.<ref>PMID:15899866</ref> [[http://www.uniprot.org/uniprot/TBP_HUMAN TBP_HUMAN]] General transcription factor that functions at the core of the DNA-binding multiprotein factor TFIID. Binding of TFIID to the TATA box is the initial transcriptional step of the pre-initiation complex (PIC), playing a role in the activation of eukaryotic genes transcribed by RNA polymerase II. Component of the transcription factor SL1/TIF-IB complex, which is involved in the assembly of the PIC (preinitiation complex) during RNA polymerase I-dependent transcription. The rate of PIC formation probably is primarily dependent on the rate of association of SL1 with the rDNA promoter. SL1 is involved in stabilization of nucleolar transcription factor 1/UBTF on rDNA.<ref>PMID:15970593</ref> [[http://www.uniprot.org/uniprot/TAF4_HUMAN TAF4_HUMAN]] Makes part of TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Potentiates transcriptional activation by the AF-2S of the retinoic acid, vitamin D3 and thyroid hormone. [[http://www.uniprot.org/uniprot/TAF10_HUMAN TAF10_HUMAN]] TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. [[http://www.uniprot.org/uniprot/TAF12_HUMAN TAF12_HUMAN]] TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription. [[http://www.uniprot.org/uniprot/TAF3_HUMAN TAF3_HUMAN]] Transcription factor TFIID is one of the general factors required for accurate and regulated initiation by RNA polymerase II. TFIID is a multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. Required in complex with TBPL2 for the differentiation of myoblasts into myocytes. The complex replaces TFIID at specific promoters at an early stage in the differentiation process. [[http://www.uniprot.org/uniprot/TAF11_HUMAN TAF11_HUMAN]] Core TAFII present in both of the previously described TFIID species which either lack or contain TAFII30 (TFIID alpha and TFIID beta respectively). [[http://www.uniprot.org/uniprot/TAF5_HUMAN TAF5_HUMAN]] TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TAFs components-TIIFD are essential for mediating regulation of RNA polymerase transcription. TAF5/TAFII100 interacts strongly with the histone H4-related TAF6/TAFII80 and the histone H3-related TAF9/TAFII31, as well as a stable complex comprised of both TAF5/TAFII80 and TAF6/TAFII31. Apparently weaker interactions of TAF5/TAFII100 with TBP, TAF1/TAFII250, TAF11/TAFII28, and TAF12/TAFII20, but not TAF7/TAFII55, also have been observed. [[http://www.uniprot.org/uniprot/TAF1_HUMAN TAF1_HUMAN]] Largest component and core scaffold of the TFIID basal transcription factor complex. Contains novel N- and C-terminal Ser/Thr kinase domains which can autophosphorylate or transphosphorylate other transcription factors. Phosphorylates TP53 on 'Thr-55' which leads to MDM2-mediated degradation of TP53. Phosphorylates GTF2A1 and GTF2F1 on Ser residues. Possesses DNA-binding activity. Essential for progression of the G1 phase of the cell cycle.<ref>PMID:2038334</ref> <ref>PMID:8450888</ref> <ref>PMID:8625415</ref> <ref>PMID:9660973</ref> <ref>PMID:9858607</ref> <ref>PMID:11278496</ref> <ref>PMID:15053879</ref> [[http://www.uniprot.org/uniprot/TAF13_HUMAN TAF13_HUMAN]] TFIID beta-specific TAFII. [[http://www.uniprot.org/uniprot/TAF6_HUMAN TAF6_HUMAN]] TAFs are components of the transcription factor IID (TFIID) complex, PCAF histone acetylase complex and TBP-free TAFII complex (TFTC). TIIFD is multimeric protein complex that plays a central role in mediating promoter responses to various activators and repressors. |
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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</div> | </div> | ||
<div class="pdbe-citations 6mzd" style="background-color:#fffaf0;"></div> | <div class="pdbe-citations 6mzd" style="background-color:#fffaf0;"></div> | ||
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+ | ==See Also== | ||
+ | *[[TATA-binding protein 3D structures|TATA-binding protein 3D structures]] | ||
+ | *[[Transcription initiation factors 3D structures|Transcription initiation factors 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
- | </ | + | </SX> |
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Large Structures]] | [[Category: Large Structures]] |
Revision as of 22:40, 6 March 2020
Human TFIID Lobe A canonical
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Categories: Homo sapiens | Large Structures | Fang, J | Greber, B J | Grunberg, S | Hahn, S | Liu, Y | Louder, R K | Luo, J | Nogales, E | Patel, A B | Ranish, J | Dna | Nuclear | Transcription