@article{RN121,
   author = {Spronk, C. A. and Tessari, M. and Kaan, A. M. and Jansen, J. F. and Vermeulen, M. and Stunnenberg, H. G. and Vuister, G. W.},
   title = {The Mad1-Sin3B interaction involves a novel helical fold},
   journal = {Nat Struct Biol},
   volume = {7},
   number = {12},
   pages = {1100-4},
   note = {Spronk, C A
Tessari, M
Kaan, A M
Jansen, J F
Vermeulen, M
Stunnenberg, H G
Vuister, G W
eng
Research Support, Non-U.S. Gov't
2000/12/02 11:00
Nat Struct Biol. 2000 Dec;7(12):1100-4. doi: 10.1038/81944.},
   abstract = {Sin3A or Sin3B are components of a corepressor complex that mediates repression by transcription factors such as the helix-loop-helix proteins Mad and Mxi. Members of the Mad/Mxi family of repressors play important roles in the transition between proliferation and differentiation by down-regulating the expression of genes that are activated by the proto-oncogene product Myc. Here, we report the solution structure of the second paired amphipathic helix (PAH) domain (PAH2) of Sin3B in complex with a peptide comprising the N-terminal region of Mad1. This complex exhibits a novel interaction fold for which we propose the name 'wedged helical bundle'. Four alpha-helices of PAH2 form a hydrophobic cleft that accommodates an amphipathic Mad1 alpha-helix. Our data further show that, upon binding Mad1, secondary structure elements of PAH2 are stabilized. The PAH2-Mad1 structure provides the basis for determining the principles of protein interaction and selectivity involving PAH domains.},
   keywords = {Amino Acid Sequence
Animals
Binding Sites
*Carrier Proteins
Cell Cycle Proteins
Conserved Sequence
Humans
Mice
Models, Molecular
Molecular Sequence Data
Nuclear Magnetic Resonance, Biomolecular
*Nuclear Proteins
Phosphoproteins/*chemistry/*metabolism
Protein Binding
Protein Structure, Secondary
Protein Structure, Tertiary
Repressor Proteins/*chemistry/*metabolism
Sequence Alignment
Solutions
Substrate Specificity
*Transcription Factors},
   ISSN = {1072-8368 (Print)
1072-8368 (Linking)},
   DOI = {10.1038/81944},
   url = {http://www.ncbi.nlm.nih.gov/pubmed/11101889
https://www.nature.com/articles/nsb1200_1100},
   year = {2000},
   type = {Journal Article}
}

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W."],"year":2000,"bibtype":"article","biburl":"https://raw.githubusercontent.com/jansenjfa1/bibbase.github.io/master/jansenjfa.bib","bibdata":{"bibtype":"article","type":"Journal Article","author":[{"propositions":[],"lastnames":["Spronk"],"firstnames":["C.","A."],"suffixes":[]},{"propositions":[],"lastnames":["Tessari"],"firstnames":["M."],"suffixes":[]},{"propositions":[],"lastnames":["Kaan"],"firstnames":["A.","M."],"suffixes":[]},{"propositions":[],"lastnames":["Jansen"],"firstnames":["J.","F."],"suffixes":[]},{"propositions":[],"lastnames":["Vermeulen"],"firstnames":["M."],"suffixes":[]},{"propositions":[],"lastnames":["Stunnenberg"],"firstnames":["H.","G."],"suffixes":[]},{"propositions":[],"lastnames":["Vuister"],"firstnames":["G.","W."],"suffixes":[]}],"title":"The Mad1-Sin3B interaction involves a novel helical fold","journal":"Nat Struct Biol","volume":"7","number":"12","pages":"1100-4","note":"Spronk, C A Tessari, M Kaan, A M Jansen, J F Vermeulen, M Stunnenberg, H G Vuister, G W eng Research Support, Non-U.S. Gov't 2000/12/02 11:00 Nat Struct Biol. 2000 Dec;7(12):1100-4. doi: 10.1038/81944.","abstract":"Sin3A or Sin3B are components of a corepressor complex that mediates repression by transcription factors such as the helix-loop-helix proteins Mad and Mxi. Members of the Mad/Mxi family of repressors play important roles in the transition between proliferation and differentiation by down-regulating the expression of genes that are activated by the proto-oncogene product Myc. Here, we report the solution structure of the second paired amphipathic helix (PAH) domain (PAH2) of Sin3B in complex with a peptide comprising the N-terminal region of Mad1. This complex exhibits a novel interaction fold for which we propose the name 'wedged helical bundle'. Four alpha-helices of PAH2 form a hydrophobic cleft that accommodates an amphipathic Mad1 alpha-helix. Our data further show that, upon binding Mad1, secondary structure elements of PAH2 are stabilized. The PAH2-Mad1 structure provides the basis for determining the principles of protein interaction and selectivity involving PAH domains.","keywords":"Amino Acid Sequence Animals Binding Sites *Carrier Proteins Cell Cycle Proteins Conserved Sequence Humans Mice Models, Molecular Molecular Sequence Data Nuclear Magnetic Resonance, Biomolecular *Nuclear Proteins Phosphoproteins/*chemistry/*metabolism Protein Binding Protein Structure, Secondary Protein Structure, Tertiary Repressor Proteins/*chemistry/*metabolism Sequence Alignment Solutions Substrate Specificity *Transcription Factors","issn":"1072-8368 (Print) 1072-8368 (Linking)","doi":"10.1038/81944","url":"http://www.ncbi.nlm.nih.gov/pubmed/11101889 https://www.nature.com/articles/nsb1200_1100","year":"2000","bibtex":"@article{RN121,\n author = {Spronk, C. A. and Tessari, M. and Kaan, A. M. and Jansen, J. F. and Vermeulen, M. and Stunnenberg, H. G. and Vuister, G. W.},\n title = {The Mad1-Sin3B interaction involves a novel helical fold},\n journal = {Nat Struct Biol},\n volume = {7},\n number = {12},\n pages = {1100-4},\n note = {Spronk, C A\nTessari, M\nKaan, A M\nJansen, J F\nVermeulen, M\nStunnenberg, H G\nVuister, G W\neng\nResearch Support, Non-U.S. Gov't\n2000/12/02 11:00\nNat Struct Biol. 2000 Dec;7(12):1100-4. doi: 10.1038/81944.},\n abstract = {Sin3A or Sin3B are components of a corepressor complex that mediates repression by transcription factors such as the helix-loop-helix proteins Mad and Mxi. Members of the Mad/Mxi family of repressors play important roles in the transition between proliferation and differentiation by down-regulating the expression of genes that are activated by the proto-oncogene product Myc. Here, we report the solution structure of the second paired amphipathic helix (PAH) domain (PAH2) of Sin3B in complex with a peptide comprising the N-terminal region of Mad1. This complex exhibits a novel interaction fold for which we propose the name 'wedged helical bundle'. Four alpha-helices of PAH2 form a hydrophobic cleft that accommodates an amphipathic Mad1 alpha-helix. Our data further show that, upon binding Mad1, secondary structure elements of PAH2 are stabilized. 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