scholarly journals Key Amino Acid Residues within the Third Membrane Domains of NR1 and NR2 Subunits Contribute to the Regulation of the Surface Delivery ofN-methyl-d-aspartate Receptors

2012 ◽  
Vol 287 (31) ◽  
pp. 26423-26434 ◽  
Author(s):  
Martina Kaniakova ◽  
Barbora Krausova ◽  
Vojtech Vyklicky ◽  
Miloslav Korinek ◽  
Katarina Lichnerova ◽  
...  
Keyword(s):  
Amino Acid ◽  
Membrane Domains ◽  
Amino Acid Residues ◽  
The Third ◽  
Nr2 Subunits

The power of the force: mechano-physiology of the giant titin

2018 ◽  
Vol 2 (5) ◽  
pp. 681-686 ◽  
Author(s):  
Jaime Andrés Rivas-Pardo
Keyword(s):  
Amino Acid ◽  
Human Body ◽  
Actin Filaments ◽  
Polypeptide Chain ◽  
Single Gene ◽  
The Other ◽  
Amino Acid Residues ◽  
The Third ◽  
Single Polypeptide Chain ◽  
Single Polypeptide

Titin — the largest protein in the human body — spans half of the muscle sarcomere from the Z-disk to the M-band through a single polypeptide chain. More than 30 000 amino acid residues coded from a single gene (TTN, in humans Q8WZ42) form a long filamentous protein organized in individual globular domains concatenated in tandem. Owing to its location and close interaction with the other muscle filaments, titin is considered the third filament of muscle, after the thick-myosin and the thin-actin filaments.

scholarly journals Characterization of the Phd Repressor-Antitoxin Boundary

2005 ◽  
Vol 187 (2) ◽  
pp. 765-770 ◽  
Author(s):  
James Estle McKinley ◽  
Roy David Magnuson
Keyword(s):  
Amino Acid ◽  
Point Mutations ◽  
Modular Organization ◽  
Amino Acid Residues ◽  
The Third ◽  
Linear Sequence ◽  
C Terminus ◽  
Overlapping Sets ◽  
Repressor Activity

ABSTRACT The P1 plasmid addiction operon (a classic toxin-antitoxin system) encodes Phd, an unstable 73-amino-acid repressor-antitoxin protein, and Doc, a stable toxin. It was previously shown by deletion analysis that the N terminus of Phd was required for repressor activity and that the C terminus was required for antitoxin activity. Since only a quarter of the protein or less was required for both activities, it was hypothesized that Phd might have a modular organization. To further test the modular hypothesis, we constructed and characterized a set of 30 point mutations in the third and fourth quarters of Phd. Four mutations (PhdA36H, V37A, I38A, and F44A) had major defects in repressor activity. Five mutations (PhdD53A, D53R, E55A, F56A, and F60A) had major defects in antitoxin activity. As predicted by the modular hypothesis, point mutations affecting each activity belonged to disjoint, rather than overlapping, sets and were separated rather than interspersed within the linear sequence. A final deletion experiment demonstrated that the C-terminal 24 amino acid residues of Phd (preceded by a methionine) retained full antitoxin activity.

scholarly journals Amino acid residues in the third alpha-helix of growth hormone involved in growth promoting activity.

1995 ◽  
Vol 9 (3) ◽  
pp. 292-302
Author(s):  
W Y Chen ◽  
N Y Chen ◽  
J Yun ◽  
D C Wight ◽  
X Z Wang ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Alpha Helix ◽  
Amino Acid Residues ◽  
The Third ◽  
Growth Promoting

Block and Modulation ofN-Methyl-d-Aspartate Receptors by Polyamines and Protons: Role of Amino Acid Residues in the Transmembrane and Pore-Forming Regions of NR1 and NR2 Subunits

1997 ◽  
Vol 52 (4) ◽  
pp. 701-713 ◽  
Author(s):  
Keiko Kashiwagi ◽  
Albert J. Pahk ◽  
Takashi Masuko ◽  
Kazuei Igarashi ◽  
Keith Williams
Keyword(s):  
Amino Acid ◽  
Amino Acid Residues ◽  
Nr2 Subunits

scholarly journals Phosphorylase kinase phosphorylation of skeletal-muscle troponin T

1980 ◽  
Vol 191 (3) ◽  
pp. 851-854 ◽  
Author(s):  
V V Risnik ◽  
A B Dobrovolskii ◽  
N B Gusev ◽  
S E Severin
Keyword(s):  
Skeletal Muscle ◽  
Amino Acid ◽  
Troponin T ◽  
Rabbit Skeletal Muscle ◽  
Phosphorylase Kinase ◽  
Amino Acid Residues ◽  
Standard Preparation ◽  
The Third ◽  
Original Preparation ◽  
Kinase Phosphorylation

Rabbit skeletal-muscle troponin T was phosphorylated by a standard preparation of phosphorylase kinase [Cohen (1973) Eur. J. Biochem. 34, 1–14] and by fractions obtained after chromatography of phosphorylase kinase on phosphocellulose. The original preparation of phosphorylase kinase phosphorylated at least two sites, one of which was serine-1. The second and probably the third sites were presumably located in the peptide flanked by amino-acid residues 147 and 161 of troponin T. Fractions of phosphorylase kinase was adsorbed on phosphocellulose phosphorylated only the second site. Tightly adsorbed fractions possessed high troponin T kinase and phosvitin kinase activities and phosphorylated only serine-1 of troponin T. The results suggest that standard preparations of phosphorylase kinase are contaminated by troponin T kinase, which can phosphorylate serine-1 of troponin T.

Specifities of Rabbit Antisera to Multiple Antigen (MAP) Peptides

1995 ◽  
Vol 50 (9-10) ◽  
pp. 735-738
Author(s):  
Alberto Chersi ◽  
Francesca di Modugno ◽  
Giuliana Falasca
Keyword(s):  
Immune Response ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
The Third ◽  
Multiple Antigen ◽  
Multiple Antigen Peptides

Abstract Two multiple antigen peptides consisting of 6 and 7 amino acid residues, respectively, plus a 12-residue fragment, used as a control, all linked to a polylysine core, were used as immunogens in rabbits in order to obtain an immune response. Rabbit antisera against such polymers were then tested in ELISA against a panel of antigens in order to analyze the specificites of the resulting antibodies. The responses were different for all three immunogens, being partially or totally directed, for two of the three compounds, including the 12-residue control MAP peptide, against the polylysyl core, which is considered as non immunogenic. The third MAP polymer was practically unable to elicit an immune response

scholarly journals Identification of Metal Ligands in theClostridium histolyticum ColH Collagenase

1999 ◽  
Vol 181 (9) ◽  
pp. 2816-2822 ◽  
Author(s):  
Chang-Min Jung ◽  
Osamu Matsushita ◽  
Seiichi Katayama ◽  
Junzaburo Minami ◽  
Jun Sakurai ◽  
...  
Keyword(s):  
Catalytic Activity ◽  
Amino Acid ◽  
Enzymatic Activity ◽  
Zinc Content ◽  
Catalytic Site ◽  
Zinc Binding ◽  
Amino Acid Residues ◽  
Conserved Residues ◽  
Metal Ligands ◽  
The Third

ABSTRACT A Clostridium histolyticum 116-kDa collagenase has an H415EXXH motif but not the third zinc ligand, as found in already characterized zinc metalloproteinases. To identify its catalytic site, we mutated the codons corresponding to the three conserved residues in the motif to other amino acid residues. The mutation affecting His415 or His419 abolished catalytic activity and zinc binding, while that affecting Glu416 did the former but not the latter. These results suggest that the motif forms the catalytic site. We also mutated the codons corresponding to other amino acid residues that are likely zinc ligands. The mutation affecting Glu447 decreased markedly both the enzymatic activity and the zinc content, while that affecting Glu446 or Glu451 had smaller effects on activity and zinc binding. These mutations caused a decrease ink cat but no significant change inKm . These results are consistent with the hypothesis that Glu447 is the third zinc ligand. The spacing of the three zinc ligands is the same in all known clostridial collagenases but not in other known gluzincins, indicating that they form a new gluzincin subfamily. The effects of mutations affecting Glu446 and Glu451 suggest that the two residues are also involved in catalysis, possibly through an interaction with the two zinc-binding histidine residues.

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