Interacting Partners for Kringle Domains Of Plasminogen: Common Binding With K1 and K5 Domains

Title: Interacting Partners for Kringle Domains Of Plasminogen: Common Binding With K1 and K5 Domains

Volume: 11 Issue: 6

Author(s): Naehyun Kong, Dongyeol Lim and Kyunghee Lee

Affiliation:

Keywords: angiostatin, kringles, yeast two hybrid

Abstract: We have identified MAZR and Rgl2 as specific interacting partners for kringle domains in angiostatin (K1-4) and K5 using yeast two hybrid screening. Both K1 and K1-4 have strong interaction with MAZR and Rgl2 whereas K5 only binds with Rgl2. No interaction of K2, K3, and K4 with either of these binding proteins was detected. We suggest that a common binding motif may exist near LBS-4 that is required for binding with Rgl2 but not with MAZR.

Cite this article as:

Kong Naehyun, Lim Dongyeol and Lee Kyunghee, Interacting Partners for Kringle Domains Of Plasminogen: Common Binding With K1 and K5 Domains, Protein & Peptide Letters 2004; 11 (6) . https://dx.doi.org/10.2174/0929866043406382