1P059 Typical structure of carbohydrate binding site
نویسندگان
چکیده
منابع مشابه
The carbohydrate-binding promiscuity of Euonymus europaeus lectin is predicted to involve a single binding site.
Euonymus europaeus lectin (EEL) is a carbohydrate-binding protein derived from the fruit of the European spindle tree. EEL was first identified for its erythrocyte agglutinating properties and specificity for B and H blood groups. However, a detailed molecular picture of the structural basis of carbohydrate recognition by EEL remains to be developed. In this study, we performed fluorescence tit...
متن کاملa typical graph structure of a ring
the zero-divisor graph of a commutative ring r with respect to nilpotent elements is a simple undirected graph $gamma_n^*(r)$ with vertex set z_n(r)*, and two vertices x and y are adjacent if and only if xy is nilpotent and xy is nonzero, where z_n(r)={x in r: xy is nilpotent, for some y in r^*}. in this paper, we investigate the basic properties of $gamma_n^*(r)$. we discuss when it will be eu...
متن کاملStructure and function of a HECT domain ubiquitin-binding site.
The Rsp5 ubiquitin ligase contains a non-covalent binding site for ubiquitin within the amino-terminal lobe (N-lobe) of the HECT domain, and the X-ray crystal structure of the HECT-ubiquitin complex has been determined. Hydrophobic patch residues of ubiquitin (L8, I44, V70) were crucial for interaction with Rsp5, and amino-acid alterations at the Rsp5-binding interface resulted in defects in po...
متن کاملCrystal structure of BrlR reveals a potential pyocyanin binding site
The transcriptional regulator BrlR from Pseudomonas aeruginosa is a member of the MerR family. Studies have shown BrlR can be activated by the secondary messenger 3′,5′-cyclic diguanylic acid (c-di-GMP) and contributes to P. aeruginosa biofilm tolerance. Previous structural analysis of BrlR-c-di-GMP complex has identified one hydrophobic pocket locating in its C-terminal GyrI-like domain. Howev...
متن کاملStructure of the antithrombin-binding site in heparin.
Heparin preparations from pig intestinal mucosa and from bovine lung were separated by chromatography on antithrombin-Sepharose into a high-affinity fraction (with high anticoagulant activity) and a low-affinity fraction (with low anticoagulant). Antithrombin-binding heparin fragments (12-16 monosaccharide units) were prepared, either by digesting a high-affinity heparin-antithrombin complex wi...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Seibutsu Butsuri
سال: 2004
ISSN: 0582-4052,1347-4219
DOI: 10.2142/biophys.44.s44_3