✦ LIBER ✦

Homology among DNA-binding proteins suggests use of a conserved super-secondary structure

✍ Scribed by Sauer, R. T.; Yocum, R. R.; Doolittle, R. F.; Lewis, M.; Pabo, C. O.

Book ID: 109727098
Publisher: Nature Publishing Group
Year: 1982
Tongue: English
Weight: 581 KB
Volume: 298
Category: Article
ISSN: 0028-0836
DOI: 10.1038/298447a0

No coin nor oath required. For personal study only.

📜 SIMILAR VOLUMES

Homology among DNA-binding proteins sugg

Homology among DNA-binding proteins suggests use of a conserved super-secondary structure

✍ Sauer, R. T.; Yocum, R. R.; Doolittle, R. F.; Lewis, M.; Pabo, C. O. 📂 Article 📅 1982 🏛 Nature Publishing Group 🌐 English ⚖ 581 KB

Sequence of a Drosophila segmentation ge

Sequence of a Drosophila segmentation gene: protein structure homology with DNA-binding proteins

✍ Laughon, Allen; Scott, Matthew P. 📂 Article 📅 1984 🏛 Nature Publishing Group 🌐 English ⚖ 804 KB

Computer-assisted primary and secondary

Computer-assisted primary and secondary structure analyses of DNA polymerases of herpes simplex, Epstein-Barr and varicella zoster viruses reveal conserved domains with some homology to DNA-binding domain inE. coliDNA pol I

✍ Yechiel Becker 📂 Article 📅 1988 🏛 Springer 🌐 English ⚖ 898 KB

PhaR, a protein of unknown function cons

PhaR, a protein of unknown function conserved among short-chain-length polyhydroxyalkanoic acids producing bacteria, is a DNA-binding protein and represses Paracoccus denitrificans phaP expression in vitro

✍ Akira Maehara; Yoshiharu Doi; Tatsuaki Nishiyama; Yasuo Takagi; Shunsaku Ueda; H 📂 Article 📅 2001 🏛 John Wiley and Sons 🌐 English ⚖ 301 KB

Structures of the platelet calcium- and

Structures of the platelet calcium- and integrin-binding protein and the αIIb-integrin cytoplasmic domain suggest a mechanism for calcium-regulated recognition; homology modelling and NMR studies

✍ P. M. Hwang; H. J. Vogel 📂 Article 📅 2000 🏛 John Wiley and Sons 🌐 English ⚖ 421 KB 👁 1 views

Calcium- and integrin-binding protein (CIB) binds to the 20-residue alphaIIb cytoplasmic domain of platelet alphaIIbbeta3 integrin. Amino acid sequence similarities with calmodulin (CaM) and calcineurin B (CnB) allowed the construction of homology-based models of calcium-saturated CIB as well as apo