Crystal structure of mouse carnosinase CN2 at 1.8 Å resolution
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چکیده
منابع مشابه
Crystal structure of human CK2α at 1.06 Å resolution
The Ser/Thr kinase CK2 consists of two catalytic subunits (CK2α) and a dimer of the regulatory subunits (CK2β), and is a ubiquitous enzyme that regulates growth, proliferation and the survival of cells. CK2 is a remarkable drug target for potentially treating a wide variety of tumours and glomerulonephritis. The purified CK2α protein was crystallized using ethylene glycol as a precipitant. The ...
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lation of phosducin reduces the stability of the phosSummary ducin/Gtbg complex (Yoshida et al., 1994), allowing Gta to reassociate promptly with Gtbg and maximizing the The crystal structure of transducin’s bg subunits comphoton signal amplification. Phosducin is dephosphoryplexed with phosducin, which regulates Gtbg activity, lated by type 1 or 2A phosphatases (Pagh-Roehl et al., has been sol...
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Mushroom tyrosinase-associated lectin-like protein (MtaL) binds to mature Agaricus bisporus tyrosinase in vivo, but the exact physiological function of MtaL is unknown. In this study, the crystal structure of recombinant MtaL is reported at 1.35 Å resolution. Comparison of its structure with that of the truncated and cleaved MtaL present in the complex with tyrosinase directly isolated from mus...
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Peptidyl-tRNA hydrolase (Pth) catalyzes the release of tRNA to relieve peptidyl-tRNA accumulation. Because Pth activity is essential for the viability of bacteria, Pth is regarded as a promising target for the discovery of new antimicrobial agents. Here, the structure of Pth from the Gram-positive bacterium Staphylococcus aureus (SaPth) was solved by X-ray crystallography at a 2.25 Å resolution...
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ژورنال
عنوان ژورنال: Acta Crystallographica Section A Foundations of Crystallography
سال: 2005
ISSN: 0108-7673
DOI: 10.1107/s0108767305090793