2ght
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(New page: 200px<br /> <applet load="2ght" size="450" color="white" frame="true" align="right" spinBox="true" caption="2ght, resolution 1.8Å" /> '''CTD-specific phospha...)
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Revision as of 20:12, 12 November 2007
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CTD-specific phosphatase Scp1 in complex with peptide from C-terminal domain of RNA polymerase II
Overview
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.
About this Structure
2GHT is a Protein complex structure of sequences from Homo sapiens with MG as ligand. Active as Phosphoprotein phosphatase, with EC number 3.1.3.16 Full crystallographic information is available from OCA.
Reference
Determinants for dephosphorylation of the RNA polymerase II C-terminal domain by Scp1., Zhang Y, Kim Y, Genoud N, Gao J, Kelly JW, Pfaff SL, Gill GN, Dixon JE, Noel JP, Mol Cell. 2006 Dec 8;24(5):759-70. PMID:17157258
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