Pub. Date : 2010 Oct 4
PMID : 20920334
4 Functional Relationships(s)Download |
Sentence | Compound Name | Protein Name | Organism |
| 1 | NMR data at atomic resolution indicate prolyl cis/trans isomerisation of the highly conserved proline residues Pro-5, -10, -14 and -35 of Vpr are catalyzed by human CypA and require only very low concentrations of the isomerase relative to that of the peptide substrates. | Proline | peptidylprolyl isomerase A | Homo sapiens |
| 2 | NMR data at atomic resolution indicate prolyl cis/trans isomerisation of the highly conserved proline residues Pro-5, -10, -14 and -35 of Vpr are catalyzed by human CypA and require only very low concentrations of the isomerase relative to that of the peptide substrates. | Proline | peptidylprolyl isomerase A | Homo sapiens |
| 3 | CONCLUSIONS: Only N-terminal peptides of Vpr containing Pro-35, which appears to be vital for manifold functions of Vpr, bind to CypA in a biosensor assay. | Proline | peptidylprolyl isomerase A | Homo sapiens |
| 4 | This indicates that Pro-35 is essential for a specific CypA-Vpr binding interaction, in contrast to the general prolyl cis/trans isomerisation observed for all proline residues of Vpr, which only involve transient enzyme-substrate interactions. | Proline | peptidylprolyl isomerase A | Homo sapiens |