Title : Maturation-induced conformational changes of HIV-1 capsid protein and identification of two high affinity sites for cyclophilins in the C-terminal domain.

Pub. Date : 1999 Feb 26

PMID : 10026140






4 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 CyPA binds to the previously identified Gly-Pro90 site of the capsid protein p24, but its role remained unclear. Glycine peptidylprolyl isomerase A Homo sapiens
2 Peptides corresponding to these regions showed higher affinities (Kd approximately 0.3 microM) for both CyPA and cyclophilin B than the best peptide derived from the Gly-Pro90 site ( approximately 8 microM) and thus revealed new sequence motifs flanking Gly-Pro that are important for tight interaction of peptide ligands with cyclophilins. Glycine peptidylprolyl isomerase A Homo sapiens
3 Peptides corresponding to these regions showed higher affinities (Kd approximately 0.3 microM) for both CyPA and cyclophilin B than the best peptide derived from the Gly-Pro90 site ( approximately 8 microM) and thus revealed new sequence motifs flanking Gly-Pro that are important for tight interaction of peptide ligands with cyclophilins. Glycine peptidylprolyl isomerase A Homo sapiens
4 Between CyPA and an immature (unprocessed) form of p24, a Kd of approximately 8 microM was measured, which corresponded with the Kd of the best of the Gly-Pro90 peptides, indicating an association via this site. Glycine peptidylprolyl isomerase A Homo sapiens