A consensus amino-acid sequence repeat in Torpedo and mammalian Ca2+-dependent membrane-binding proteins

Nature ◽  
1986 ◽  
Vol 320 (6063) ◽  
pp. 636-638 ◽  
Author(s):  
Michael J. Geisow ◽  
Ulrich Fritsche ◽  
J. Mark Hexham ◽  
Bret Dash ◽  
Tolu Johnson
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Proteins ◽  
Membrane Binding ◽  
Sequence Repeat ◽  
Consensus Amino Acid Sequence ◽  
Consensus Amino Acid

scholarly journals Asparagine Linked Oligosaccharides Present on a Non‐Consensus Amino Acid Sequence in the CH1 Domain of Human Antibodies

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
John F. Valliere‐Douglass ◽  
Catherine M. Eakin ◽  
Paul Kodama ◽  
Mirna Mujacic ◽  
Lowell J. Brady ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Antibodies ◽  
Consensus Amino Acid Sequence ◽  
Consensus Amino Acid

scholarly journals Asparagine-linked Oligosaccharides Present on a Non-consensus Amino Acid Sequence in the CH1 Domain of Human Antibodies

2009 ◽  
Vol 284 (47) ◽  
pp. 32493-32506 ◽  
Author(s):  
John F. Valliere-Douglass ◽  
Paul Kodama ◽  
Mirna Mujacic ◽  
Lowell J. Brady ◽  
Wes Wang ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Human Antibodies ◽  
Consensus Amino Acid Sequence ◽  
Consensus Amino Acid

scholarly journals Molecular Modeling of Epithiospecifier and Nitrile-Specifier Proteins of Broccoli and Their Interaction with Aglycones

Molecules ◽  
2020 ◽  
Vol 25 (4) ◽  
pp. 772 ◽  
Author(s):  
Juan Román ◽  
Dorian González ◽  
Mario Inostroza-Ponta ◽  
Andrea Mahn
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Three Dimensional ◽  
Dimensional Structure ◽  
Plant Metabolites ◽  
Secondary Plant Metabolites ◽  
Consensus Amino Acid Sequence ◽  
The Stability ◽  
Dynamics Simulations ◽  
Consensus Amino Acid

Glucosinolates are secondary plant metabolites of Brassicaceae. They exert their effect after enzymatic hydrolysis to yield aglycones, which become nitriles and epithionitriles through the action of epithiospecifier (ESP) and nitrile-specifier proteins (NSP). The mechanism of action of broccoli ESP and NSP is poorly understood mainly because ESP and NSP structures have not been completely characterized and because aglycones are unstable, thus hindering experimental measurements. The aim of this work was to investigate the interaction of broccoli ESP and NSP with the aglycones derived from broccoli glucosinolates using molecular simulations. The three-dimensional structure of broccoli ESP was built based on its amino-acid sequence, and the NSP structure was constructed based on a consensus amino-acid sequence. The models obtained using Iterative Threading ASSEmbly Refinement (I-TASSER) were refined with the OPLS-AA/L all atom force field of GROMACS 5.0.7 and were validated by Veryfy3D and ERRAT. The structures were selected based on molecular dynamics simulations. Interactions between the proteins and aglycones were simulated with Autodock Vina at different pH. It was concluded that pH determines the stability of the complexes and that the aglycone derived from glucoraphanin has the highest affinity to both ESP and NSP. This agrees with the fact that glucoraphanin is the most abundant glucosinolate in broccoli florets.

scholarly journals Three distinct anti-allergic drugs, amlexanox, cromolyn and tranilast, bind to S100A12 and S100A13 of the S100 protein family

1999 ◽  
Vol 338 (3) ◽  
pp. 583-589 ◽  
Author(s):  
Tsuyoshi SHISHIBORI ◽  
Yuhta OYAMA ◽  
Osamu MATSUSHITA ◽  
Kayoko YAMASHITA ◽  
Hiromi FURUICHI ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Calcium Binding ◽  
Binding Proteins ◽  
S100 Protein ◽  
Reversed Phase ◽  
Molecular Probes ◽  
Calcium Binding Proteins ◽  
Ige Mediated ◽  
Human And Mouse

To investigate the roles of calcium-binding proteins in degranulation, we used three anti-allergic drugs, amlexanox, cromolyn and tranilast, which inhibit IgE-mediated degranulation of mast cells, as molecular probes in affinity chromatography. All of these drugs, which have different structures but similar function, scarcely bound to calmodulin in bovine lung extract, but bound to the same kinds of calcium-binding proteins, such as the 10-kDa proteins isolated in this study, calcyphosine and annexins I–V. The 10-kDa proteins obtained on three drug-coupled resins and on phenyl-Sepharose were analysed by reversed-phase HPLC. It was found that two characteristic 10-kDa proteins, one polar and one less polar, were bound with all three drugs, although S100A2 (S100L), of the S100 family, was bound with phenyl-Sepharose. The cDNA and deduced amino acid sequence proved our major polar protein to be identical with the calcium-binding protein in bovine amniotic fluid (CAAF1, S100A12). The cDNA and deduced amino acid sequence of the less-polar protein shared 95% homology with human and mouse S100A13. In addition, it was demonstrated that the native S100A12 and recombinant S100A12 and S100A13 bind to immobilized amlexanox. On the basis of these findings, we speculate that the three anti-allergic drugs might inhibit degranulation by binding with S100A12 and S100A13.

scholarly journals Chitin-binding proteins in potato (Solanum tuberosum L.) tuber. Characterization, immunolocalization and effects of wounding

1992 ◽  
Vol 283 (3) ◽  
pp. 813-821 ◽  
Author(s):  
D J Millar ◽  
A K Allen ◽  
C G Smith ◽  
C Sidebottom ◽  
A R Slabas ◽  
...  
Keyword(s):  
Solanum Tuberosum ◽  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Proteins ◽  
Solanum Tuberosum L ◽  
Major Protein ◽  
Post Translational Modification ◽  
Terminal Amino Acid ◽  
Terminal Amino ◽  
Terminal Amino Acid Sequence

Tubers of potato (Solanum tuberosum L.) contain a number of chitin-binding proteins which have possible functions in defence against pathogens. A major protein of the tuber is the chitin-binding lectin which has been further characterized with respect to its antigenicity and N-terminal amino acid sequence. By using an antiserum monospecific for tuber lectin in unwounded potato the protein was found in the cytoplasm and vacuole, unusually for a hydroxyproline-rich glycoprotein, but consistent with its soluble nature in subcellular extracts. Little increased synthesis of the lectin precursor or the post-translationally modified form could be demonstrated in excised potato tuber discs. However, after wounding there is increased synthesis of another hydroxyproline-containing glycoprotein of Mr 57,000, which binds to chitin and shares common epitopes with the lectin. In comparison with the tuber lectin, this novel glycoprotein contains less hydroxyproline, but from its overall composition it is clearly not an underhydroxylated form of the tuber lectin. It differed in its N-terminal amino acid sequence and was much less glycosylated, although arabinose was still present. Synthesis of the Mr-57,000 polypeptide began after the initial burst of protein synthesis and increased, reaching a peak at 24 h after wounding. The protein was produced with its enzymes of post-translational modification, prolyl hydroxylase and arabinosyltransferase, concomitantly with the marker enzymes for wounding, phenylalanine ammonia-lyase and membrane-bound phenol oxidase and peroxidase.

Molecular cloning of the cDNA for stimulatory GDP/GTP exchange protein for smg p21s (ras p21-like small GTP-binding proteins) and characterization of stimulatory GDP/GTP exchange protein

1991 ◽  
Vol 11 (5) ◽  
pp. 2873-2880
Author(s):  
K Kaibuchi ◽  
T Mizuno ◽  
H Fujioka ◽  
T Yamamoto ◽  
K Kishi ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Exchange Reaction ◽  
Binding Proteins ◽  
Bovine Brain ◽  
Rat Tissues ◽  
Gtp Binding Proteins ◽  
Gtp Binding ◽  
Ras P21 ◽  
Exchange Protein

We have recently purified to near homogeneity the stimulatory GDP/GTP exchange protein for smg p21s (ras p21-like GTP-binding proteins) from bovine brain cytosol. This regulatory protein, named GDP dissociation stimulator (GDS), stimulates the GDP/GTP exchange reaction of smg p21s by stimulating the dissociation of GDP from and the subsequent binding of GTP to them. In this study, we have isolated and sequenced the cDNA of smg p21 GDS from a bovine brain cDNA library by using an oligonucleotide probe designed from the partial amino acid sequence of the purified smg p21 GDS. The cDNA has an open reading frame encoding a protein of 558 amino acids with a calculated Mr value of 61,066, similar to the Mr of 53,000 estimated for the purified smg p21 GDS by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and sucrose density gradient ultracentrifugation. The isolated cDNA is expressed in Escherichia coli, and the encoded protein exhibits smg p21 GDS activity. smg p21 GDS is overall hydrophilic, but there are several short hydrophobic regions. The smg p21 GDS mRNA is present in bovine brain and various rat tissues. smg p21 GDS has low amino acid sequence homology with the yeast CDC25 and SCD25 proteins, which may regulate the GDP/GTP exchange reaction of the yeast RAS2 protein, but not with ras p21 GTPase-activating protein, the inhibitory GDP/GTP exchange proteins (GDP dissociation inhibitor) for smg p25A and rho p21s, and the beta gamma subunits of heterotrimeric GTP-binding proteins such as Gs and Gi.

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