1 - 10 of 26 articles
Protein tyrosine phosphatase-basophil like (PTP-BL) represents a large multi domain non-transmembrane scaffolding protein that contains five PDZ domains. Here we report the backbone assignments of the PDZ2/PDZ3 tandem domain of PTP-BL. These assignments now provide a basis for the detailed...
Connexin40 is a gap junction protein involved in cell communication in the heart and other tissues. The assignments of an important Connexin40 regulatory domain, the carboxyl terminus, will aid in identifying the types of inter- and intramolecular interactions that affect channel activity.
An allotypic variation at position 25 influences the fibrillogenicity of λVI light chains, which are related to humoral immune response and have been associated with AL amyloidosis. The full resonance assignment and a preliminary structural characterization of 6aJL2(R25G) are reported.
The HSP100/AAA+ superfamily protein ClpC is a key regulator of cell development in Bacillus subtilis. We present here the backbone and side-chain assignments of the N-terminal repeat domain (residues 1–145) of ClpC from Bacillus subtilis.
13C, 15N, and 1H chemical shift assignments are presented for the cAMP-regulated phosphoprotein endosulfine-alpha in its free and micelle-bound states. Secondary chemical shift analysis demonstrates formation of four helices in the micelle-bound state, which are not present in the absence of...
Chemerin is a potent chemoattractant for cells expressing the GPCR CMKLR1, and is thought to play important roles in cell migration and recruitment to sites of tissue damage and inflammation. Here we report the NMR assignments of the 15.6 kDa active form of uniformly 15N, 13C labeled chemerin.
The backbone and side chain assignments of the retroviral aspartate protease from Simian Foamy Virus from macaques (SFVmac) have been determined by triple resonance NMR techniques.
In order to determine the structure of the 15 kDa cyclic nucleotide binding domain of a cyclic nucleotide-activated K+ channel from Mesorhizobium loti and its interaction with cAMP, nearly complete 1H, 13C, and 15N chemical shifts were assigned.
We report NMR assignments of the protein backbone of the C-terminal domain (163 a.a.) of human class 1 translation termination factor eRF1. It was found that several protein loop residues exist in two slowly interconverting conformational states.
We report the full resonance assignments of MOD, which is an active mutant of maize ribosome-inactivating protein (mRIP). mRIP is a unique RIP which is synthesized as an inactive precursor and processed by removal of an internal inactivation region to yield an active form.
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