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Molecular mechanism and structural basis of interactions of dipeptidyl peptidase IV with adenosine deaminase and human immunodeficiency virus type-1 transcription transactivator

H. Fan, F. L. Tansi, W. Weihofen, W. A. Wilhelm, C. Böttcher, J. Hu, J. Martinez, W. Saenger, and W. Reutter – 2012

Dipeptidyl peptidase IV (DPPIV or CD26) is a multifunctional membrane glycoprotein. As an exopeptidase it regulates the activity of a series of biologically important peptides. Through its interaction with specific proteins and peptides. DPPIV is also involved in a wide range of biologically relevant processes such as cell adhesion, T cell activation and apoptosis. In this paper, we review our recent studies on the interactions of DPPIV with adenosine deaminase (ADA) and the transcription transactivator of the human immunodeficiency virus type-1 (HIV-1 Tat) as revealed by three-dimensional structure reconstructed by single particle analysis of cryo-electron microscopy (EM) and crystal structures of the human DPPIV-bovine ADA complex as well as the crystal structures of DPPIV in complex with HIV-1 Tat-derived nona peptides. These results contribute importantly to the clarification of the molecular mechanisms of this multifunctional protein. The biological relevance of these interactions is discussed. (C) 2011 Elsevier GmbH. All rights reserved.

Titel
Molecular mechanism and structural basis of interactions of dipeptidyl peptidase IV with adenosine deaminase and human immunodeficiency virus type-1 transcription transactivator
Verfasser
H. Fan, F. L. Tansi, W. Weihofen, W. A. Wilhelm, C. Böttcher, J. Hu, J. Martinez, W. Saenger, and W. Reutter
Datum
2012
Kennung
DOI: 10.1016/j.ejcb.2011.06.001
Zitierweise
Eur. J. Cell Biol. 2012, 91, 265 - 273
Sprache
eng
Art
Text