The Solution Structure of 18 residue YH motif Peptide within the Second fas-1 domain of βig-h3
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βig-h3 is an extracellular matrix protein that mediates cell adhesion through interaction with integrins. The 18 residue YH motifs within each fas-1 domain are known to be responsible for the interaction with the αvβ5 integrin, and the synthetic YH motif peptides are known to inhibit endothelial tube formation and reduces the number of blood vessels, and so expected to be an effective inhibitor of angiogenesis. In this study, we solved the 3D structure of the 18 residue YH motif peptide (EALRDLLNNHILKSAMCA; D2 peptide) within the second fas-1 domain of βig-h3 using NMR. The Peptide has α-helix structure at the C terminal region but the N terminal region is flexible. The present structural information may be helpful for developing more effective peptide drug candidate for the treatment of diseases dependent on angiogenesis.
Abstract
βig-h3 is an extracellular matrix protein that mediates cell adhesion through interaction with integrins. The 18 residue YH motifs within each fas-1 domain are known to be responsible for the interaction with the αvβ5 integrin, and the synthetic YH motif peptides are known to inhibit endothelial tube formation and reduces the number of blood vessels, and so expected to be an effective inhibitor of angiogenesis. In this study, we solved the 3D structure of the 18 residue YH motif peptide (EALRDLLNNHILKSAMCA; D2 peptide) within the second fas-1 domain of βig-h3 using NMR. The Peptide has α-helix structure at the C terminal region but the N terminal region is flexible. The present structural information may be helpful for developing more effective peptide drug candidate for the treatment of diseases dependent on angiogenesis.
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