Biological Function and Chemistry of Endothelin. A Review

1999 ◽  
Vol 64 (8) ◽  
pp. 1211-1252 ◽  
Author(s):  
Jan Hlaváček ◽  
Renáta Marcová
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Biological Function ◽  
Biological Properties ◽  
Structural Basis ◽  
Amino Acid Residues ◽  
Snake Venoms ◽  
Vasoactive Peptides ◽  
Physico Chemical ◽  
Endothelin A

The first part of this review deals with the biosynthesis and a biological function of strongly vasoactive peptides named endothelins (ETs) including vasoactive intestinal contractor. Where it was useful, snake venoms sarafotoxins which are structural endothelin derivatives, were also mentioned. In the second part, an attention is paid to structural basis of the ETs biological activity, with respect to alterations of amino acid residues in the parent peptides modifying the conformation and consequently the physico-chemical and biological properties in corresponding ETs analogs. Special attention is focussed on the area of ETs receptors and their interaction with peptide and non peptide agonists and antagonists, important in designing selective inhibitors of ETs receptors potentially applicable as drugs in a medicine. A review with 182 references.

scholarly journals Evolution-Based Functional Decomposition of Proteins

2015 ◽  
Author(s):  
Olivier Rivoire ◽  
Kimberly A. Reynolds ◽  
Rama Ranganathan
Keyword(s):  
Amino Acid ◽  
Protein Function ◽  
Biological Properties ◽  
Protein Family ◽  
Structural Basis ◽  
Amino Acid Residues ◽  
Multiple Sequence ◽  
Global Pattern ◽  
Sector Analysis ◽  
Statistical Coupling

The essential biological properties of proteins - folding, biochemical activities, and the capacity to adapt - arise from the global pattern of interactions between amino acid residues. The statistical coupling analysis (SCA) is an approach to defining this pattern that involves the study of amino acid coevolution in an ensemble of sequences comprising a protein family. This approach indicates a functional architecture within proteins in which the basic units are coupled networks of amino acids termed sectors. This evolution-based decomposition has potential for new understandings of the structural basis for protein function, but requires broad further testing by the scientific community. To facilitate this, we present here the principles and practice of the SCA and introduce new methods for sector analysis in a python-based software package. We show that the pattern of amino acid interactions within sectors is linked to the divergence of functional lineages in a multiple sequence alignment - a model for how sector properties might be differentially tuned in members of a protein family. This work provides new tools for understanding the structural basis for protein function and for generally testing the concept of sectors as the principal functional units of proteins.

Metal complexes of polymers with amino acid residues. formation, stability and controlled biological activity

1990 ◽  
Vol 14 (1) ◽  
pp. 61-70 ◽  
Author(s):  
V.A. Lee ◽  
R.I. Musin ◽  
R.I. Tashmukhamedov ◽  
M.I. Shtilman ◽  
S.Sh. Rashidova
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Metal Complexes ◽  
Amino Acid Residues

The effect of modifications of the A5 and A19 amino acid residues on the biological activity of insulin. [Leu5-A] and [Phe19-A] sheep insulins

1983 ◽  
Vol 2 (2) ◽  
pp. 147-170 ◽  
Author(s):  
Nicolaos Ferderigos ◽  
G. Thompson Burke ◽  
Kouki Kitagawa ◽  
Panayotis G. Katsoyannis
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Residues

scholarly journals Human red blood cell Wright antigens: a genetic and evolutionary perspective on glycophorin A-band 3 interaction

Blood ◽  
1996 ◽  
Vol 87 (9) ◽  
pp. 3942-3947 ◽  
Author(s):  
CH Huang ◽  
ME Reid ◽  
SS Xie ◽  
OO Blumenfeld
Keyword(s):  
Amino Acid ◽  
Nonhuman Primates ◽  
Antigen Expression ◽  
Band 3 ◽  
Structural Basis ◽  
Antigenic Structure ◽  
Glycophorin A ◽  
Amino Acid Residues ◽  
Protein Protein Interaction ◽  
Human Red Blood Cells

The Wright (Wra/Wrb) blood group polymorphism is defined by an allelic change (Lys658Glu) in the band 3 protein; nevertheless, the Wrb antigen apparently requires glycophorin A (GPA) for surface presentation. To gain insight into the structural basis for this protein-protein interaction and delineate its relationship with Wrb antigen expression, we investigated GPA and band 3 sequence polymorphisms occurring in rare humans and nonhuman primates. The lack of GPA or amino acid residues 59 through 71 of GPA results in the absence of Wrb from human red blood cells (RBCs) exhibiting the MkMk, En(a-), or MiV phenotype. However, the SAT homozygous cells carried a Glu658 form of band 3 and a hybrid glycophorin with the entire GPA extramembrane domain from residues 1 through 71, yet expressed no Wrb antigen. This finding suggests that formation of the Wrb antigenic structure is dependent on protein folding and that the transmembrane junction of GPA is important in maintaining the required conformation. Comparative analyses of GPA and band 3 homologues led to the identification in the interacting regions of conserved and dispensable amino acid residues that correlated with the Wrb positive or negative status on nonhuman primates. In particular, the chimpanzee RBCs cells expressed Wrb and the Glu658 form of band 3, which is identical to humans, but their GPA contained the Gly rather than Arg residue at position 61. Taken together, the results suggest that (1) Arg61 of GPA and the proposed Arg61-Glu658 charge pair are not crucial for Wrb antigen exhibition and (2) the role of GPA for interaction with band 3, including Glu658, probably involves a number of amino acid residues located in the alpha-helical region and transmembrane junction.

Structure-activity studies of dermorphin. The role of side chains of amino acid residues on the biological activity of dermorphin

Peptides ◽  
1984 ◽  
Vol 5 (4) ◽  
pp. 687-689 ◽  
Author(s):  
Krzysztof Darłak ◽  
Zbigniew Grzonka ◽  
Pawel Krzaścik ◽  
Piotr Janicki ◽  
S.Witold Gumułka
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Side Chains ◽  
Amino Acid Residues ◽  
Structure Activity

scholarly journals Identification of Amino Acid Residues Critical for Biological Activity in Human Interleukin-18

2002 ◽  
Vol 277 (13) ◽  
pp. 10998-11003 ◽  
Author(s):  
Soo-Hyun Kim ◽  
Tania Azam ◽  
Daniela Novick ◽  
Do-Young Yoon ◽  
Leonid L. Reznikov ◽  
...  
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Interleukin 18

Interaction between the A2 and A19 amino acid residues is of critical importance for high biological activity in insulin: [19-leucine-A]insulin

Biochemistry ◽  
1984 ◽  
Vol 23 (19) ◽  
pp. 4444-4448 ◽  
Author(s):  
Kouki Kitagawa ◽  
Hiroshi Ogawa ◽  
G. Thompson Burke ◽  
Jacob D. Chanley ◽  
Panayotis G. Katsoyannis
Keyword(s):  
Biological Activity ◽  
Amino Acid ◽  
Amino Acid Residues ◽  
Critical Importance ◽  
High Biological Activity

scholarly journals Inferring amino acid interactions underlying protein function

2017 ◽  
Author(s):  
Victor H. Salinas ◽  
Rama Ranganathan
Keyword(s):  
Amino Acid ◽  
Protein Function ◽  
Structural Basis ◽  
Evolutionary Divergence ◽  
Amino Acid Residues ◽  
Homologous Proteins ◽  
Physical Constraints ◽  
Spatially Distributed ◽  
Statistical Coupling ◽  
Energetic Interactions

Protein function arises from a poorly defined pattern of cooperative energetic interactions between amino acid residues. Strategies for deducing this pattern have been proposed, but lack of benchmark data has limited experimental verification. Here, we extend deep-mutation technologies to enable measurement of many thousands of pairwise amino acid couplings in members of a protein family. The data show that despite great evolutionary divergence, homologous proteins conserve a sparse, spatially distributed network of cooperative interactions between amino acids that underlies function. This pattern is quantitatively captured in the coevolution of amino acid positions, especially as indicated by the statistical coupling analysis (SCA), providing experimental confirmation of the key tenets of this method. This work establishes a clear link between physical constraints on protein function and sequence analysis, enabling a general practical approach for understanding the structural basis for protein function.

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