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Title: Determination of the core sequence of an antagonist of selectin-dependent leukocyte adhesion and correlation of its structure with molecular modeling studies. Author: Kruszynski M, Nakada MT, Tam SH, Taylor AH, Fieles WE, Heavner GA. Journal: Arch Biochem Biophys; 1996 Jul 01; 331(1):23-30. PubMed ID: 8660679. Abstract: The sequence 36-50 from the lectin domain of human P-selectin has been previously identified as a weak inhibitor of selectin-dependent leukocyte adhesion. A series of C- and N-terminally truncated peptides was synthesized to determine the limits of the active core region within the parent sequence. Deletions from both the N- and C-termini gave significant increases in inhibitory activity and identified 41-50 or 36-49 as minimum active sequences, but surprisingly not the common 41-49 peptide. All peptides tested showed parallel inhibition of both P- and E-selectin-dependent adhesion. A molecular model of the lectin domain was constructed using homology modeling. Examination of this model suggests one hypothesis to explain the increase in activity on deletion of Asp36.[Abstract] [Full Text] [Related] [New Search]