منابع مشابه
Kinking the coiled coil--negatively charged residues at the coiled-coil interface.
The coiled coil is one of the most common protein-structure motifs. It is believed to be adopted by 3-5% of all amino acids in proteins. It comprises two or more alpha-helical chains wrapped around one another. The sequences of most coiled coils are characterized by a seven-residue (heptad) repeat, denoted (abcdefg)(n). Residues at the a and d positions define the helical interface (core) and a...
متن کاملAn Undecided Coiled Coil
Leucine zippers are oligomerization domains used in a wide range of proteins. Their structure is based on a highly conserved heptad repeat sequence in which two key positions are occupied by leucines. The leucine zipper of the cell cycle-regulated Nek2 kinase is important for its dimerization and activation. However, the sequence of this leucine zipper is most unusual in that leucines occupy on...
متن کاملA seven-helix coiled coil.
Coiled-coil proteins contain a characteristic seven-residue sequence repeat whose positions are designated a to g. The interacting surface between alpha-helices in a classical coiled coil is formed by interspersing nonpolar side chains at the a and d positions with hydrophilic residues at the flanking e and g positions. To explore how the chemical nature of these core amino acids dictates the o...
متن کاملSolving coiled-coil protein structures
The successful approach to solving crystal structures of coiled-coil proteins with the program AMPLE is discussed.
متن کاملThe structure of the GemC1 coiled coil and its interaction with the Geminin family of coiled-coil proteins
GemC1, together with Idas and Geminin, an important regulator of DNA-replication licensing and differentiation decisions, constitute a superfamily sharing a homologous central coiled-coil domain. To better understand this family of proteins, the crystal structure of a GemC1 coiled-coil domain variant engineered for better solubility was determined to 2.2 Å resolution. GemC1 shows a less typical...
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ژورنال
عنوان ژورنال: Nature
سال: 1991
ISSN: 0028-0836,1476-4687
DOI: 10.1038/351188a0