Structure of an Enzyme-Derived Phosphoprotein Recognition Domain
نویسندگان
چکیده
منابع مشابه
Structure of an Enzyme-Derived Phosphoprotein Recognition Domain
Membrane Associated Guanylate Kinases (MAGUKs) contain a protein interaction domain (GK(dom)) derived from the enzyme Guanylate Kinase (GK(enz)). Here we show that GK(dom) from the MAGUK Discs large (Dlg) is a phosphoprotein recognition domain, specifically recognizing the phosphorylated form of the mitotic spindle orientation protein Partner of Inscuteable (Pins). We determined the structure o...
متن کاملStructure of the dimerization domain of the rabies virus phosphoprotein.
The crystal structure of the dimerization domain of rabies virus phosphoprotein was determined. The monomer consists of two alpha-helices that make a helical hairpin held together mainly by hydrophobic interactions. The monomer has a hydrophilic and a hydrophobic face, and in the dimer two monomers pack together through their hydrophobic surfaces. This structure is very different from the dimer...
متن کاملCrystal structure of the nipah virus phosphoprotein tetramerization domain.
The Nipah virus phosphoprotein (P) is multimeric and tethers the viral polymerase to the nucleocapsid. We present the crystal structure of the multimerization domain of Nipah virus P: a long, parallel, tetrameric, coiled coil with a small, α-helical cap structure. Across the paramyxoviruses, these domains share little sequence identity yet are similar in length and structural organization, sugg...
متن کاملAn efficient finite difference time domain algorithm for band structure calculations of Phononic crystal
In this paper, a new algorithm for studying elastic wave propagation in the phononic crystals is presented. At first, the displacement-based forms of elastic wave equations are derived and then the forms are discretized using finite difference method. So the new algorithm is called the displacement-based finite difference time domain (DBFDTD). Three numerical examples are computed with this met...
متن کاملCrystal structure of the oligomerization domain of the phosphoprotein of vesicular stomatitis virus.
In the replication cycle of nonsegmented negative-strand RNA viruses, the viral RNA-dependent RNA polymerase (L) recognizes a nucleoprotein (N)-enwrapped RNA template during the RNA polymerase reaction. The viral phosphoprotein (P) is a polymerase cofactor essential for this recognition. We report here the 2.3-angstroms-resolution crystal structure of the central domain (residues 107 to 177) of...
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: PLoS ONE
سال: 2012
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0036014