Reference : Cyclophilin a binds to linear peptide motifs containing a consensus that is present i...
Scientific journals : Other
Life sciences : Biochemistry, biophysics & molecular biology
http://hdl.handle.net/10993/3773
Cyclophilin a binds to linear peptide motifs containing a consensus that is present in many human proteins
English
Piotukh, K. [> >]
Gu, Wei mailto []
Kofler, M. [> >]
Labudde, D. [> >]
Helms, V. [> >]
Freund, C. [> >]
2005
Journal of Biological Chemistry
American Society for Biochemistry and Molecular Biology
280
25
23668-23674
Yes (verified by ORBilu)
International
0021-9258
1083-351X
Baltimore
MD
[en] Cyclophilin A ( CypA) is a peptidyl-prolyl cis/trans-isomerase that is involved in multiple signaling events of eukaryotic cells. It might either act as a catalyst for prolyl bond isomerization, or it can form stoichiometric complexes with target proteins. We have investigated the linear sequence recognition code for CypA by phage display and found the consensus motif FGPXLp to be selected after five rounds of panning. The peptide FGP-DLPAGD showed inhibition of the isomerase reaction and NMR chemical shift mapping experiments highlight the CypA interaction epitope. Ligand docking suggests that the peptide was able to bind to CypA in the cis- and trans-conformation. Protein Data Bank searches reveal that many human proteins contain the consensus motif, and several of these protein motifs are shown to interact with CypA in vitro. These sequences represent putative target sites for binding of CypA to intracellular proteins.
http://hdl.handle.net/10993/3773
10.1074/jbc.M503405200

File(s) associated to this reference

Fulltext file(s):

FileCommentaryVersionSizeAccess
Limited access
J. Biol. Chem.-2005-Piotukh-23668-74.pdfPublisher postprint1.15 MBRequest a copy

Bookmark and Share SFX Query

All documents in ORBilu are protected by a user license.