Interacting partners for kringle domains of plasminogen: common binding with K1 and K5 domains.
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.
Kong
Naehyun
N
Department of Applied Chemistry, Sejong University, 98 Gunja-Dong, Gwangjin-Gu, Seoul 143-747, South Korea.
Lim
Dongyeol
D
Lee
Kyunghee
K
D043168:Angiostatins / Q000378:metabolism*; D000818:Animals; D020662:Guanine Nucleotide Exchange Factors; D018082:Kringles / Q000502:physiology*; D051379:Mice; D009363:Neoplasm Proteins / Q000378:metabolism; D010958:Plasminogen / Q000378:metabolism*; D011485:Protein Binding / Q000502:physiology; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000378:metabolism; D014157:Transcription Factors / Q000378:metabolism; D020798:Two-Hybrid System Techniques
D020662:Guanine Nucleotide Exchange Factors; D009363:Neoplasm Proteins; D012097:Repressor Proteins; C490805:Rgl2 protein, mouse; D014157:Transcription Factors; C485875:Zfp278 protein, mouse; D043168:Angiostatins; D010958:Plasminogen