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The histidine triad superfamily of nucleotide-binding proteins.

The histidine triad superfamily of nucleotide-binding proteins. Research Abstract Details 

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  • The histidine triad superfamily of nucleotide-binding proteins. Abstract Text:

    c brennerC Brenner,p bieganowskiP Bieganowski,h c paceH C Pace,k huebnerK Huebner,

    Histidine triad (HIT) proteins were until recently a superfamily of proteins that shared only sequence motifs. Crystal structures of nucleotide-bound forms of histidine triad nucleotide-binding protein (Hint) demonstrated that the conserved residues in HIT proteins are responsible for their distinctive, dimeric, 10-stranded half-barrel structures that form two identical purine nucleotide-binding sites. Hint-related proteins, found in all forms of life, and fragile histidine triad (Fhit)-related proteins, found in animals and fungi, represent the two main branches of the HIT superfamily. Hint homologs are intracellular receptors for purine mononucleotides whose cellular function remains elusive. Fhit homologs bind and cleave diadenosine polyphosphates (Ap(n)A) such as ApppA and AppppA. Fhit-Ap(n)A complexes appear to function in a proapoptotic tumor suppression pathway in epithelial tissues. In invertebrates, Fhit homologs are encoded as fusion proteins with proteins related to plant and bacterial nitrilases that are candidate signaling partners in tumor suppression.

    The histidine triad superfamily of nucleotide-binding proteins. Publishing Authors By Initials

    c brennerC Brenner,p bieganowskiP Bieganowski,hc paceHC Pace,k huebnerK Huebner,

    For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: sequence homology: sequence homology, amino acid research

    PUBMED ID PMID:

    MEDLINE DATE:

    The histidine triad superfamily of nucleotide-binding proteins. Journal Published:

    PUBLICATION TYPE: Review

    Journal: Journal of cellular physiology

    VOLUME: 181

    Page Numbers: 179-87

    Journal Abbreviation: J. Cell. Physiol.

    ISSN: 0021-9541

    DAY: 25

    MONTH: Nov

    YEAR: 1999

    The histidine triad superfamily of nucleotide-binding proteins. Information

    Number of References: 54

    LANGUAGE: eng

    NlmUniqueID: 50222

    The histidine triad superfamily of nucleotide-binding proteins. Keywords Mesh Terms:

    KEYWORDS: Sequence Homology, Amino Acid

    MESH TERMS: metabolism

    Chemical & Substance for Abstract: The histidine triad superfamily of nucleotide-binding proteins. Information

    Substance Name: Hydrolases

    Registry Number: EC 3.-

    Grant and Affiliation Information for The histidine triad superfamily of nucleotide-binding proteins.

    AFFILIATION: Kimmel Cancer Institute, Thomas Jefferson University, Philadelphia, Pennsylvania, USA.

    Country: UNITED STATES

    UNITED STATES Research PublicationUNITED STATES Research Publication

    AGENCY: United States NCI

    GRANT: R01 CA075954-03

    ACRONYM: CA

    MEDLINETA: J Cell Physiol

    REFSOURCE:

    DATABASENAME:

    ACCESSION NUMBER:

    Number Hits: 0

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