Binding of the LXCXE Insulin Motif to a Hexapeptide Derived from Retinoblastoma Protein

• Published in: Biochemical and biophysical research communications Vol. 206; no. 1; pp. 97 - 102
• Main Authors: Radulescu, R.T., Bellitti, M.R., Ruvo, M., Cassani, G., Fassina, G.
• Format: Journal Article
• Language: English
• Published: United States Elsevier Inc 05.01.1995
• Subjects: Amino Acid Sequence; Chromatography, Affinity; Enzyme-Linked Immunosorbent Assay; Humans; Insulin - chemistry; Insulin - metabolism; Kinetics; Molecular Sequence Data; Oncogene Proteins, Viral - chemistry; Oncogene Proteins, Viral - metabolism; Papillomaviridae; Papillomavirus E7 Proteins; Peptide Fragments - chemical synthesis; Peptide Fragments - chemistry; Peptide Fragments - metabolism; Retinoblastoma Protein - chemistry; Retinoblastoma Protein - metabolism; Structure-Activity Relationship
• ISSN: 0006-291X; 1090-2104
• DOI: 10.1006/bbrc.1995.1014

Peptides corresponding to retinoblastoma protein (RB) fragment 649-654 (LFYKKV) were tested for their ability to recognize the LXCXE sequence motif in human papilloma virus type 16E7 protein (HPV-16E7) encompassing E7 residues 21-26 (DLYCYE) and an identical motif in human insulin comprising insulin B-chain residues 16-21 (YLVCGE), respectively. Interaction between these complementary peptide sequences was observed by several approaches, including direct and competitive ELISA as well as affinity chromatography. Moreover, we demonstrated that immobilized RB649-654 displays specific recognition properties towards full-length insulin. Hence, this study provides a first experimental support for the previously anticipated complex formation between insulin and RB.