N-terminal HIV-1 Tat nonapeptides as inhibitors of dipeptidyl peptidase IV. Conformational characterization

Advances in Experimental Medicine and Biology

Volumn 477, Issue , 2000, Pages 125-129

  Mrestani Klaus, Carmen ^a   Fengler, Annett ^a   Faust, Jürgen ^a   Brandt, Wolfgang ^a   Wrenger, Sabine ^b   Reinhold, Dirk ^b   Ansorge, Siegfried ^b   Neubert, Klaus ^a  

^a MARTIN LUTHER UNIVERSITY HALLE WITTENBERG   (Germany)

^b OTTO VON GUERICKE UNIVERSITY   (Germany)

Author keywords

1H NMR spectroscopy; Dipeptidyl peptidase IV; DP IV inhibitors; HIV 1 Tat; MD calculations

Indexed keywords

DIPEPTIDYL PEPTIDASE IV; NONAPEPTIDE; TRANSACTIVATOR PROTEIN;

CONFERENCE PAPER; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; ENZYME INHIBITOR INTERACTION; HUMAN IMMUNODEFICIENCY VIRUS 1; INHIBITION KINETICS; MOLECULAR INTERACTION; NONHUMAN; PRIORITY JOURNAL; PROTON NUCLEAR MAGNETIC RESONANCE;

AMINO ACID SUBSTITUTION; ANIMALS; ANTIGENS, CD26; GENE PRODUCTS, TAT; HIV-1; HUMANS; IMMUNE SYSTEM; MAGNETIC RESONANCE SPECTROSCOPY; PEPTIDE FRAGMENTS; PROTEIN BINDING; PROTEIN CONFORMATION; SERINE PROTEINASE INHIBITORS; SWINE;

HUMAN IMMUNODEFICIENCY VIRUS; HUMAN IMMUNODEFICIENCY VIRUS 1;

EID: 0034473468     PISSN: 00652598     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (6)

1. Human immunodeficiency virus 1 Tat binds to dipeptidyl aminopeptidase IV (CD26): A possible mechanism for Tat's immunosuppressive activity
2. 1H NMR conformational study on N-terminal nonapeptide sequences of HIV-1 Tat protein: A contribution to structure-activity relationships
3. Coassociation of CD26 (dipeptidyl peptidase IV) with CD45 on the surface of human T lymphocytes
4. The N-terminal X-X-Pro sequence of the HIV-1 Tat protein is important for the inhibition of dipeptidyl peptidase IV (DP IV/CD26) and the suppression of mitogen-induced proliferation of human T cells
5. The N-terminal structure of HIV-1 Tat is required for suppression of CD26-dependent T cell growth