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| {{STRUCTURE_2ghq| PDB=2ghq | SCENE= }} | | {{STRUCTURE_2ghq| PDB=2ghq | SCENE= }} |
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| '''CTD-specific phosphatase Scp1 in complex with peptide C-terminal domain of RNA polymerase II'''
| | ===CTD-specific phosphatase Scp1 in complex with peptide C-terminal domain of RNA polymerase II=== |
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| ==Overview==
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| Phosphorylation and dephosphorylation of the C-terminal domain (CTD) of RNA polymerase II (Pol II) represent a critical regulatory checkpoint for transcription. Transcription initiation requires Fcp1/Scp1-mediated dephosphorylation of phospho-CTD. Fcp1 and Scp1 belong to a family of Mg2+ -dependent phosphoserine (P.Ser)/phosphothreonine (P.Thr)-specific phosphatases. We recently showed that Scp1 is an evolutionarily conserved regulator of neuronal gene silencing. Here, we present the X-ray crystal structures of a dominant-negative form of human Scp1 (D96N mutant) bound to mono- and diphosphorylated peptides encompassing the CTD heptad repeat (Y1S2P3T4S5P6S7). Moreover, kinetic and thermodynamic analyses of Scp1-phospho-CTD peptide complexes support the structures determined. This combined structure-function analysis discloses the residues in Scp1 involved in CTD binding and its preferential dephosphorylation of P.Ser5 of the CTD heptad repeat. Moreover, these results provide a template for the design of specific inhibitors of Scp1 for the study of neuronal stem cell development.
| | The line below this paragraph, {{ABSTRACT_PUBMED_17157258}}, adds the Publication Abstract to the page |
| | (as it appears on PubMed at http://www.pubmed.gov), where 17157258 is the PubMed ID number. |
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| | {{ABSTRACT_PUBMED_17157258}} |
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| ==About this Structure== | | ==About this Structure== |
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| [[Category: Had superfamily]] | | [[Category: Had superfamily]] |
| [[Category: Protein-peptide complex]] | | [[Category: Protein-peptide complex]] |
| ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 05:07:16 2008'' | | |
| | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Jul 29 11:00:45 2008'' |