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Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity.

Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Research Abstract Details 

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  • Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Abstract Text:

    yizhou liuYizhou Liu,wei chenWei Chen,justin gaudetJustin Gaudet,matthew d cheneyMatthew D Cheney,liya roudaiaLiya Roudaia,tomasz cierpickiTomasz Cierpicki,rachel c kletRachel C Klet,kari hartmanKari Hartman,thomas m laueThomas M Laue,nancy a speckNancy A Speck,john h bushwellerJohn H Bushweller,

    AML1/ETO results from the t(8;21) associated with 12%-15% of acute myeloid leukemia. The AML1/ETO MYND domain mediates interactions with the corepressors SMRT and N-CoR and contributes to AML1/ETO's ability to repress proliferation and differentiation of primary bone marrow cells as well as to enhance their self renewal in vitro. We solved the solution structure of the MYND domain and show it to be structurally homologous to the PHD and RING finger families of proteins. We also determined the solution structure of an MYND-SMRT peptide complex. We demonstrated that a single amino acid substitution that disrupts the interaction between the MYND domain and the SMRT peptide attenuated AML1/ETO's effects on proliferation, differentiation, and gene expression.

    Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Publishing Authors By Initials

    y liuY Liu,w chenW Chen,j gaudetJ Gaudet,md cheneyMD Cheney,l roudaiaL Roudaia,t cierpickiT Cierpicki,rc kletRC Klet,k hartmanK Hartman,tm laueTM Laue,na speckNA Speck,jh bushwellerJH Bushweller,

    For similar proteins: transcription factors: repressor proteins research abstracts see: proteins: transcription factors: repressor proteins research

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    Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Journal Published:

    PUBLICATION TYPE: Research Support, N.I.H., Extr

    Journal: Cancer cell

    VOLUME: 11

    Page Numbers: 483-97

    Journal Abbreviation: Cancer Cell

    ISSN: 1535-6108

    DAY: 3

    MONTH: Jun

    YEAR: 2007

    Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Information

    Number of References:

    LANGUAGE: eng

    NlmUniqueID: 101130617

    Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Keywords Mesh Terms:

    KEYWORDS: Repressor Proteins

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity. Information

    Substance Name: nuclear receptor co-repressor 1

    Registry Number: 0

    Grant and Affiliation Information for Structural basis for recognition of SMRT/N-CoR by the MYND domain and its contribution to AML1/ETO's activity.

    AFFILIATION: Department of Molecular Physiology and Biological Physics, University of Virginia, Charlottesville, VA 22906, USA.

    Country: United States

    United States Research PublicationUnited States Research Publication

    AGENCY: United States NIGMS

    GRANT: T32 GM08704

    ACRONYM: GM

    MEDLINETA: Cancer Cell

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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