Ludwig_2004_Biochem.Biophys.Res.Commun_313_223

Reference

Title : 3D structure of the CD26-ADA complex obtained by cryo-EM and single particle analysis - Ludwig_2004_Biochem.Biophys.Res.Commun_313_223
Author(s) : Ludwig K , Fan H , Dobers J , Berger M , Reutter W , Bottcher C
Ref : Biochemical & Biophysical Research Communications , 313 :223 , 2004
Abstract :

The specific binding of adenosine deaminase to the multifunctional membrane glycoprotein dipeptidyl peptidase IV is thought to be immunologically relevant for certain regulatory and co-stimulatory processes. In this study we present the 3D structure of the complete CD26-ADA complex obtained by single particle cryo-EM at 22A resolution. ADA binding occurs at the outer edges of the beta-propeller of CD26. Docking calculations of available CD26 and ADA crystal data into the obtained EM density map revealed that the ADA-binding site is stretched across CD26 beta-propeller blades 4 and 5 involving the outermost distal hydrophobic amino acids L294 and V341 but not T440 and K441 as suggested by antibody binding. Though the docking of the ADA orientation appears less significant due to the lack of distinct surface features, non-ambiguous conclusions can be drawn in the combination with earlier indirect non-imaging methods affirming the crucial role of the ADA alpha2-helix for binding.

PubMedSearch : Ludwig_2004_Biochem.Biophys.Res.Commun_313_223
PubMedID: 14684150

Related information

Citations formats

Ludwig K, Fan H, Dobers J, Berger M, Reutter W, Bottcher C (2004)
3D structure of the CD26-ADA complex obtained by cryo-EM and single particle analysis
Biochemical & Biophysical Research Communications 313 :223

Ludwig K, Fan H, Dobers J, Berger M, Reutter W, Bottcher C (2004)
Biochemical & Biophysical Research Communications 313 :223