The 2.12Å crystal structure shows that the peptide forms a cyclic structure with a disulfide bond.
These new results highlight how small structural differences allow different ligand binding specificity even within conserved receptor families.
The 2.12Å crystal structure shows that the peptide forms a cyclic structure with a disulfide bond.
These new results highlight how small structural differences allow different ligand binding specificity even within conserved receptor families.
The 2.12Å crystal structure shows that the peptide forms a cyclic structure with a disulfide bond.
These new results highlight how small structural differences allow different ligand binding specificity even within conserved receptor families.
The 2.12Å crystal structure shows that the peptide forms a cyclic structure with a disulfide bond.
These new results highlight how small structural differences allow different ligand binding specificity even within conserved receptor families.
So far, this conserved family of receptors was only known to bind linear peptides.
Find the previous paper by @jackrhodes.bsky.social et al below 👇
So far, this conserved family of receptors was only known to bind linear peptides.
Find the previous paper by @jackrhodes.bsky.social et al below 👇