The C-Terminal Domain of α-Spectrin is Structurally Related to Calmodulin
✍ Scribed by Gilles Travé; Annalisa Pastore; Marko Hyvönen; Matti Saraste
- Book ID
- 115131639
- Publisher
- John Wiley and Sons
- Year
- 1995
- Tongue
- English
- Weight
- 967 KB
- Volume
- 227
- Category
- Article
- ISSN
- 1432-1327
No coin nor oath required. For personal study only.
📜 SIMILAR VOLUMES
## Abstract Calmodulin (CaM) is a Ca^2+^‐binding protein that functions as a ubiquitous Ca^2+^‐signaling molecule, through conformational changes from the “closed” apo conformation to the “open” Ca^2+^‐bound conformation. Mg^2+^ also binds to CaM and stabilizes its folded structure, but the NMR sig
The α subunit C-terminal domain (αCTD) of RNA polymerase (RNAP) is a key element in transcription activation in__Escherichia coli__, possessing determinants responsible for the interaction of RNAP with DNA and with transcription factors. Here, the crystal structure of__E. coli__αCTD (α subunit resid