Identifying Residues that Determine SCF Molecular-Level Interactions through a Combination of Experimental and In silico Analyses

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• 作者：Eitan Rabinovich¹ ; Michael Heyne¹ ; ² ; Anna Bakhman³ ; Mickey Kosloff³ ; Julia M. Shifman² ; Niv Papo¹ ; ^{papo@bgu.ac.il}
• 关键词：PPI ; protein&ndash ; protein interaction ; YSD ; yeast surface display ; FACS ; fluorescence-activated cell sorting ; SCF ; stem cell factor ; SCFWT ; SCF wild-type ; PE ; phycoerythrin ; SPR ; surface plasmon resonance ; FDPB ; finite-difference Poisson&ndash ; Boltzmann ; LB-Amp ; Luria Broth-Ampicillin ; BSA ; bovine serum albumin ; RU ; response unit
• 刊名：Journal of Molecular Biology
• 出版年：2017
• 出版时间：6 January 2017
• 年：2017
• 卷：429
• 期：1
• 页码：97-114
• 全文大小：1915 K
• 卷排序：429

文摘

Identifying SCF residues crucial to SCF/c-Kit interactions is key for understanding signaling. SCF residues crucial for binding can be distant from the c-Kit binding site. Combined computational–combinatorial method maps and explains crucial interactions. Core residues reduce binding affinity indirectly or via protein destabilization.