Document 0087
 DOCN  M95B0087
 TI    Complete 1H nuclear magnetic resonance assignments and structural
       characterization of a fusion protein of the alpha-amylase inhibitor
       tendamistat with the activation domain of the human immunodeficiency
       virus type 1 Tat protein.
 DT    9511
 AU    Freund J; Vertesy L; Koller KP; Wolber V; Heintz D; Kalbitzer HR;
       Max-Planck-Institute for Medical Research, Department of; Biophysics,
       Heidelberg, Germany.
 SO    J Mol Biol. 1995 Jul 28;250(5):672-88. Unique Identifier : AIDSLINE
       MED/95349076
 AB    Complete sequence-specific assignments of the 1H-NMR spectrum of a
       fusion protein of the alpha-amylase inhibitor tendamistat from
       Streptomyces tendae and the activation domain of Tat from human
       immunodeficiency virus type 1 (HIV-1) was obtained by homonuclear
       two-dimensional NMR methods. The protein behaves as expected for an
       ideal fusion protein: the flexible linker allows an almost completely
       decoupled motion of the subunits of the protein and the two subunits
       show almost no mutual interaction. In the tendamistat part, small
       structural distortions due to exchange of the carboxy-terminal leucine
       propagate mainly via the hydrogen bonds of the beta-sheet and the
       disulfide bond. The Tat part of the protein contains the seven cysteine
       residues of full-length Tat. The fusion protein was expressed in
       Streptomyces lividans and exported. During the export to the
       extracellular space disulfide bonds are created by the expressing cells,
       only one sulfhydryl group remains accessible for sulfhydryl reagents.
       Although a unique, dominant conformation with a specific disulfide
       bonding pattern exists, a significant conformational variation can be
       observed including cis-proline peptide bonds, which may indicate smaller
       populations with alternative disulfide bonding patterns.
 DE    alpha-Amylase/*ANTAGONISTS & INHIB  Amino Acid Sequence  Escherichia
       coli  Gene Products, tat/*CHEMISTRY/GENETICS  Human  Hydrogen Bonding
       Hydrogen-Ion Concentration  HIV-1/*CHEMISTRY/GENETICS  Molecular
       Sequence Data  Molecular Structure  Nuclear Magnetic Resonance
       Peptides/*CHEMISTRY/GENETICS  Recombinant Fusion Proteins/CHEMISTRY
       Streptomyces/CHEMISTRY  Sulfur/CHEMISTRY  Support, Non-U.S. Gov't
       Temperature  JOURNAL ARTICLE

       SOURCE: National Library of Medicine.  NOTICE: This material may be
       protected by Copyright Law (Title 17, U.S.Code).