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Structure and function of HIV-1 and SIV Tat proteins based on carboxy-terminal truncations, chimeric Tat constructs, and NMR modeling

✍ Scribed by G Baier-Bitterlich; A Tretiakova; MW Richardson; K Khalili; B Jameson; J Rappaport

Book ID
117576268
Publisher
Elsevier Science
Year
1998
Tongue
English
Weight
984 KB
Volume
52
Category
Article
ISSN
0753-3322

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✍ Carmen Mrestani-Klaus; Annett Fengler; Wolfgang Brandt; Jürgen Faust; Sabine Wre 📂 Article 📅 1998 🏛 John Wiley and Sons 🌐 English ⚖ 164 KB

On the basis of our recent results, the N-terminal sequence of HIV-1 Tat protein as a natural competitive inhibitor of dipeptidyl peptidase IV (DP IV) is supposed to interact directly with the active site of DP IV hence mediating its immunosuppressive effects via specific DP IV interactions. Of spec