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

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.

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On the distribution of amino acid residues in transmembrane alpha-helix bundles.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.92.10.4577 ◽

1995 ◽

Vol 92 (10) ◽

pp. 4577-4581 ◽

Cited By ~ 41

Author(s):

F. A. Samatey ◽

C. Xu ◽

J. L. Popot

Keyword(s):

Amino Acid ◽

Alpha Helix ◽

Amino Acid Residues

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Primary Structure and Anticandidal Activity of the Major Histatin from Parotid Secretion of the Subhuman Primate, Macaca fascicularis

Journal of Dental Research ◽

10.1177/00220345900690110301 ◽

1990 ◽

Vol 69 (11) ◽

pp. 1717-1723 ◽

Cited By ~ 24

Author(s):

T. Xu ◽

E. Telser ◽

R.F. Troxler ◽

F.G. Oppenheim

Keyword(s):

Amino Acid ◽

High Performance ◽

Macaca Fascicularis ◽

Sequence Similarity ◽

Gel Filtration ◽

Alpha Helix ◽

Reversed Phase ◽

Amino Acid Residues ◽

Beta Turns ◽

Anticandidal Activity

A major macaque histatin (M-histatin 1) from the parotid secretion of the subhuman primate, Macaca fascicularis, was isolated by gel filtration on Bio-Gel P-2 and purified to homogeneity by reversed-phase high-performance liquid chromatography on a TSK-ODS C18 column. The complete amino acid sequence of M-histatin 1, determined by automated Edman degradation, is: 1 10 20 Asp-Pse-His-Glu-Glu-Arg-His-His-Gly-Arg-His-Gly-His-His-Lys-Tyr-Gly-Arg-Lys-Phe 21 30 38 His-Glu-Lys-His-His-Ser-His-Arg-Gly-Tyr-Arg-Ser-Asn-Tyr-Leu-Tyr-Asp-Asn M-histatin 1 contains 38 amino acid residues, a phosphoserine at residue 2, has a molecular weight of 4881.8, a calculated pI of 8.5, and histidine forms 26.3% of the mass. The hydropathicity plot of M-histatin 1 predicts that the molecule is entirely hydrophilic, and Chou-Fasman secondary prediction indicates that the polypeptide is devoid of alpha-helix and beta-sheet conformation in aqueous solutions but contains a series of beta turns. M-histatin 1 includes a six-amino-acid insert (residue 10-15) not present in human histatins and, with the introduction of gaps to maximize homology, it displays 89% and 91% sequence similarity with human histatins 1 and 3, respectively. M-histatin 1 exhibited fungicidal and fungistatic effects against the dimorphic pathogen, Candida albicans, in three separate bioassays. Its anticandidal effects were comparable with or greater than those of human histatins 1, 3, and 5. M-histatins 2, 3, and 4 were not sequenced directly because insufficient materials were available, but the amino acid composition of M-histatin 3 was nearly identical to that of the N-terminal 20 amino acid residues of M-histatin 1. There appears to be only one major histatin in macaque parotid secretion in contrast to the family of histatins in human parotid and submandibular secretions, and the significance of this in the context of evolution and mechanism of action in anticandidal assays is discussed.

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Human pituitary growth hormone: a biologically active hendekakaihekaton peptide fragment corresponding to amino-acid residues 15-125 in the hormone molecule.

Proceedings of the National Academy of Sciences ◽

10.1073/pnas.72.10.3878 ◽

1975 ◽

Vol 72 (10) ◽

pp. 3878-3882 ◽

Cited By ~ 9

Author(s):

C. H. Li

Keyword(s):

Growth Hormone ◽

Amino Acid ◽

Biologically Active ◽

Amino Acid Residues ◽

Peptide Fragment ◽

Human Pituitary ◽

Pituitary Growth Hormone

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In silico prediction of the functional and structural consequences of the non-synonymous single nucleotide polymorphism A122V in bovine CXC chemokine receptor type 1

Brazilian Journal of Biology ◽

10.1590/1519-6984.188655 ◽

2020 ◽

Vol 80 (1) ◽

pp. 39-46

Author(s):

A. F. Guzzi ◽

F. S. L. Oliveira ◽

M. M. S. Amaro ◽

P. F. Tavares-Filho ◽

J. E. Gabriel

Keyword(s):

Amino Acid ◽

Chemokine Receptor ◽

In Silico ◽

Alpha Helix ◽

Amino Acid Sequences ◽

Receptor Type ◽

Amino Acid Residues ◽

Causal Polymorphism ◽

Cxc Chemokine

Abstract The current study aimed to assess whether the A122V causal polymorphism promotes alterations in the functional and structural proprieties of the CXC chemokine receptor type 1 protein (CXCR1) of cattle Bos taurus by in silico analyses. Two amino acid sequences of bovine CXCR1 was selected from database UniProtKB/Swiss-Prot: a) non-polymorphic sequence (A7KWG0) with alanine (A) at position 122, and b) polymorphic sequence harboring the A122V polymorphism, substituting alanine by valine (V) at same position. CXCR1 sequences were submitted as input to different Bioinformatics’ tools to examine the effects of this polymorphism on functional and structural stabilities, to predict eventual alterations in the 3-D structural modeling, and to estimate the quality and accuracy of the predictive models. The A122V polymorphism exerted tolerable and non-deleterious effects on the polymorphic CXCR1, and the predictive structural model for polymorphic CXCR1 revealed an alpha helix spatial structure typical of a receptor transmembrane polypeptide. Although higher variations in the distances between pairs of amino acid residues at target-positions are detected in the polymorphic CXCR1 protein, more than 97% of the amino acid residues in both models were located in favored and allowed conformational regions in Ramachandran plots. Evidences has supported that the A122V polymorphism in the CXCR1 protein is associated with increased clinical mastitis incidence in dairy cows. Thus, the findings described herein prove that the replacement of the alanine by valine amino acids provokes local conformational changes in the A122V-harboring CXCR1 protein, which could directly affect its post-translational folding mechanisms and biological functionality.

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Characterization of the Phd Repressor-Antitoxin Boundary

Journal of Bacteriology ◽

10.1128/jb.187.2.765-770.2005 ◽

2005 ◽

Vol 187 (2) ◽

pp. 765-770 ◽

Cited By ~ 19

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.

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Bovine growth hormone fragment (1–133) has in-vitro somatomedin-like activity

Journal of Endocrinology ◽

10.1677/joe.0.0960195 ◽

1983 ◽

Vol 96 (2) ◽

pp. 195-199 ◽

Cited By ~ 8

Author(s):

J. P. Liberti ◽

L. A. Durham

Keyword(s):

Growth Hormone ◽

Amino Acid ◽

Costal Cartilage ◽

Peptide Bond ◽

Biologically Active ◽

The Other ◽

Bovine Growth Hormone ◽

Amino Acid Residues ◽

In Vitro Uptake

Thrombin digestion of bovine growth hormone (1–191) resulted in cleavage of the peptide bond between amino acid residues 133 and 134. Native growth hormone and purified peptides (1–133) and (134–191) were assayed for somatomedin-like activity. Peptide (1–133), ranging in concentration from 0·15–15 nmol/l, stimulated in-vitro uptake of [3H]thymidine by rat costal cartilage. None of the other peptides was biologically active.

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Capsid Protein C of Tick-Borne Encephalitis Virus Tolerates Large Internal Deletions and Is a Favorable Target for Attenuation of Virulence

Journal of Virology ◽

10.1128/jvi.76.7.3534-3543.2002 ◽

2002 ◽

Vol 76 (7) ◽

pp. 3534-3543 ◽

Cited By ~ 97

Author(s):

Regina M. Kofler ◽

Franz X. Heinz ◽

Christian W. Mandl

Keyword(s):

Amino Acid ◽

Capsid Protein ◽

Protein C ◽

Alpha Helix ◽

Helical Conformation ◽

Amino Acid Residues ◽

Structural Class ◽

Hydrophobic Domain ◽

Tick Borne Encephalitis ◽

Subviral Particles

ABSTRACT Deletions ranging in size from 4 to 21 amino acid residues were introduced into the capsid protein of the flavivirus tick-borne encephalitis (TBE) virus. These deletions incrementally affected a hydrophobic domain which is present at the center of all flavivirus capsid protein sequences and part of which may form an amphipathic alpha-helix. In the context of the full-length TBE genome, the deletions did not measurably affect protein expression and up to a deletion length of 16 amino acid residues, corresponding to almost 17% of mature protein C, viable virus was recovered. This virus was strongly attenuated but highly immunogenic in adult mice, revealing capsid protein C as a new and attractive target for the directed attenuation of flaviviruses. Apparently, the larger deletions interfered with the correct assembly of infectious virus particles, and this disturbance of virion assembly is likely to be the molecular basis of attenuation. However, all of the mutants carrying large deletions produced substantial amounts of subviral particles, which as judged from density gradient analyses were identical to recombinant subviral particles as obtained by the expression of the surface proteins prM and E alone. The structural and functional flexibility of protein C revealed in this study and its predicted largely alpha-helical conformation are reminiscent of capsid proteins of other enveloped viruses, such as alphaviruses (N-terminal domain of the capsid protein), retroviruses, and hepadnaviruses and suggest that all of these may belong to a common structural class, which is fundamentally distinct from the classical β-barrel structures of many icosahedral viral capsids. The possibility of attenuating flaviviruses by disturbing virus assembly and favoring the production of noninfectious but highly immunogenic subviral particles opens up a promising new avenue for the development of live flavivirus vaccines.

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