Fan_2012_Eur.J.Cell.Biol_91_265

Reference

Title : Molecular mechanism and structural basis of interactions of dipeptidyl peptidase IV with adenosine deaminase and human immunodeficiency virus type-1 transcription transactivator - Fan_2012_Eur.J.Cell.Biol_91_265
Author(s) : Fan H , Tansi FL , Weihofen WA , Bottcher C , Hu J , Martinez J , Saenger W , Reutter W
Ref : European Journal of Cell Biology , 91 :265 , 2012
Abstract :

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 nonapeptides. These results contribute importantly to the clarification of the molecular mechanisms of this multifunctional protein. The biological relevance of these interactions is discussed.

PubMedSearch : Fan_2012_Eur.J.Cell.Biol_91_265
PubMedID: 21856036

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Citations formats

Fan H, Tansi FL, Weihofen WA, Bottcher C, Hu J, Martinez J, Saenger W, Reutter W (2012)
Molecular mechanism and structural basis of interactions of dipeptidyl peptidase IV with adenosine deaminase and human immunodeficiency virus type-1 transcription transactivator
European Journal of Cell Biology 91 :265

Fan H, Tansi FL, Weihofen WA, Bottcher C, Hu J, Martinez J, Saenger W, Reutter W (2012)
European Journal of Cell Biology 91 :265