Key result
Proper oligomerization of Ang1 having at least four subunits by intermolecular disulfide linkage involving cysteines 41 and 54 is critical for Tie2 binding and activation.
Oligomerization of Ang1 into at least tetramers via specific cysteine disulfide linkages is essential for its ability to bind and activate the Tie2 receptor, providing key insights into angiogenesis mechanisms.
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Ang1 tetramerization via specific cysteines may guide angiogenic therapies; leaves open clinical translation from animal data.
Kim et al. (2005) studied this question. Angiopoietin-1 (Ang1) and Angiopoietin-2 (Ang2) variants vs. Wild-type Ang1 and Ang2 was evaluated on Tie2 binding and activation. Proper oligomerization of Ang1 having at least four subunits by intermolecular disulfide linkage involving cysteines 41 and 54 is critical for Tie2 binding and activation.