Solution Structure of the Chicken Cysteine-Rich Protein, CRP1, a Double-LIM Protein Implicated in Muscle Differentiation

详细信息    查看全文

• 作者：Xiang Yao ; Gabriela C. Pé ; rez-Alvarado ; Heather A. Louis ; Pascal Pomiè ; s ; Catherine Hatt ; Michael F. Summers ; and Mary C. Beckerle
• 刊名：Biochemistry
• 出版年：1999
• 出版时间：May 4, 1999
• 年：1999
• 卷：38
• 期：18
• 页码：5701 - 5713
• 全文大小：344K
• 年卷期：v.38,no.18(May 4, 1999)
• ISSN：1520-4995

文摘

The mechanism by which the contractile machinery of muscle is assembled and maintained isnot well-understood. Members of the cysteine-rich protein (CRP) family have been implicated in theseprocesses. Three vertebrate CRPs (CRP1-3) that exhibit developmentally regulated muscle-specificexpression have been identified. All three proteins are associated with the actin cytoskeleton, and one hasbeen shown to be required for striated muscle structure and function. The vertebrate CRPs identified todate display a similar molecular architecture; each protein is comprised of two tandemly arrayed LIMdomains, protein-binding motifs found in a number of proteins with roles in cell differentiation. EachLIM domain coordinates two Zn(II) ions that are bound independently in CCHC (C=Cys, H=His) andCCCC modules. Here we describe the solution structure of chicken CRP1 determined by homonuclearand ¹H-¹⁵N heteronuclear magnetic resonance spectroscopy. Comparison of the structures of the two LIMdomains of CRP1 reveals a high degree of similarity in their tertiary folds. In addition, the two componentLIM domains represent two completely independent folding units and exhibit no apparent interactionswith each other. The structural independence and spatial separation of the two LIM domains of CRP1 arecompatible with an adapter or linker role for the protein.