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2 results on '"šid"'

1. Differential binding of Sin3 interacting repressor domains to the PAH2 domain of Sin3A

Author

Pang, Yuan-Ping, Kumar, Ganesh A., Zhang, Jin-San, and Urrutia, Raul

Subjects
*PROTEINS, *GROWTH factors, *PEPTIDES
Abstract

The Sin3 interacting domain (SID), originally described in the Mad family of repressors, is a novel transcriptional repressor domain that binds the PAH2 domain of corepressors Sin3A and Sin3B with high affinities. The conserved SID-like domains are reportedly present in five KLF proteins. However, the KLF SIDs and the Mad SIDs can be classified into two subtypes according to sequence similarity. Here, we report the finding from computational and experimental studies that the two subtypes of SID domains bind differentially to Sin3A. This finding offers insights into a mechanism of cell growth regulation by interactions of different subtypes of SID-containing repressor proteins with Sin3. It also provides the structural basis for developing selective modulators of Sin3. [Copyright &y& Elsevier]

Published
2003
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2. Differential binding of Sin3 interacting repressor domains to the PAH2 domain of Sin3A

Author

Ganesh A. Kumar, Raul Urrutia, Jin San Zhang, and Yuan Ping Pang

Subjects
Models, Molecular, Saccharomyces cerevisiae Proteins, Biophysics, Kruppel-Like Transcription Factors, Mutation, Missense, Repressor, Cell Cycle Proteins, Plasma protein binding, KLF protein, Biology, Biochemistry, Histone Deacetylases, KLF11, Conserved sequence, Protein structure, Structural Biology, Transcription (biology), Genetics, SIN3A, Computer Simulation, Binding site, Molecular Biology, Conserved Sequence, Zinc finger, SID, Binding Sites, Nuclear Proteins, Cell Biology, Phosphoproteins, Zinc finger protein, Protein Structure, Tertiary, Repressor Proteins, Sin3 Histone Deacetylase and Corepressor Complex, Mutagenesis, Site-Directed, Trans-Activators, Apoptosis Regulatory Proteins, Mad1, Transcription, Protein Binding, Transcription Factors
Abstract

The Sin3 interacting domain (SID), originally described in the Mad family of repressors, is a novel transcriptional repressor domain that binds the PAH2 domain of corepressors Sin3A and Sin3B with high affinities. The conserved SID-like domains are reportedly present in five KLF proteins. However, the KLF SIDs and the Mad SIDs can be classified into two subtypes according to sequence similarity. Here, we report the finding from computational and experimental studies that the two subtypes of SID domains bind differentially to Sin3A. This finding offers insights into a mechanism of cell growth regulation by interactions of different subtypes of SID-containing repressor proteins with Sin3. It also provides the structural basis for developing selective modulators of Sin3.

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