2phg | pdb_00002phg

Model for VP16 binding to TFIIB

spinqualitylabelsall models 2phg, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2phg is a 2 chain structure with sequence from Homo sapiens and Viruses. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Related: 1tfb, 2phe Gene: GTF2B, TF2B, TFIIB (Homo sapiens), UL48 (Viruses) Resources: FirstGlance, OCA, RCSB, PDBsum Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMed Herpes simplex virion protein 16 (VP16) contains two strong activation regions that can independently and cooperatively activate transcription in vivo. We have identified the regions and residues involved in the interaction with the human transcriptional coactivator positive cofactor 4 (PC4) and the general transcription factor TFIIB. NMR and biochemical experiments revealed that both VP16 activation regions are required for the interaction and undergo a conformational transition from random coil to alpha-helix upon binding to its target PC4. The interaction is strongly electrostatically driven and the binding to PC4 is enhanced by the presence of its amino-terminal domain. We propose models for binding of VP16 to the core domains of PC4 and TFIIB that are based on two independent docking approaches using NMR chemical shift changes observed in titration experiments. The models are consistent with results from site-directed mutagenesis and provide an explanation for the contribution of both acidic and hydrophobic residues for transcriptional activation by VP16. Both intrinsically unstructured activation domains are attracted to their interaction partner by electrostatic interactions, and adopt an alpha-helical conformation around the important hydrophobic residues. The models showed multiple distinct binding surfaces upon interaction with various partners, providing an explanation for the promiscuous properties, cooperativity, and the high activity of this activation domain. Structural properties of the promiscuous VP16 activation domain.,Jonker HR, Wechselberger RW, Boelens R, Folkers GE, Kaptein R Biochemistry. 2005 Jan 25;44(3):827-39. PMID:15654739 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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