Refined three-dimensional solution structure of a snake cardiotoxin: Analysis of the side-chain organization suggests the existence of a possible phospholipid binding site

Biopolymers ◽  
1993 ◽  
Vol 33 (11) ◽  
pp. 1659-1675 ◽  
Author(s):  
Bernard Gilquin ◽  
Christian Roumestand ◽  
Sophie Zinn-Justin ◽  
André Ménez ◽  
Flavio Toma
Keyword(s):  
Binding Site ◽  
Solution Structure ◽  
Three Dimensional ◽  
Side Chain ◽  
Dimensional Solution ◽  
Phospholipid Binding ◽  
Chain Organization

Three-Dimensional Solution Structure ofSaccharomyces cerevisiaeReduced Iso-1-cytochromec†

Biochemistry ◽  
1996 ◽  
Vol 35 (43) ◽  
pp. 13788-13796 ◽  
Author(s):  
Paolo Baistrocchi ◽  
Lucia Banci ◽  
Ivano Bertini ◽  
Paola Turano ◽  
Kara L. Bren ◽  
...  
Keyword(s):  
Solution Structure ◽  
Three Dimensional ◽  
Dimensional Solution

scholarly journals Amino acids important in enzyme activity and dimer stability for Drosophila alcohol dehydrogenase

1995 ◽  
Vol 308 (2) ◽  
pp. 419-423 ◽  
Author(s):  
S W Chenevert ◽  
N G Fossett ◽  
S H Chang ◽  
I Tsigelny ◽  
M E Baker ◽  
...  
Keyword(s):  
Enzyme Activity ◽  
Alcohol Dehydrogenase ◽  
Binding Site ◽  
Aspartic Acid ◽  
Three Dimensional ◽  
Side Chain ◽  
Wild Type ◽  
Dimensional Model ◽  
Three Dimensional Model ◽  
Substrate Binding Site

We have determined the nucleotide sequences of eight ethyl methanesulphonate-induced mutants in Drosophila alcohol dehydrogenase (ADH), of which six were previously characterized by Hollocher and Place [(1988) Genetics 116, 253-263 and 265-274]. Four of these ADH mutants contain a single amino acid change: glycine-17 to arginine, glycine-93 to glutamic acid, alanine-159 to threonine, and glycine-184 to aspartic acid. Although these mutants are inactive, three mutants (Gly17Arg, Gly93Glu and Gly184Asp) form stable homodimers, as well as heterodimers with wild-type ADH, in which the wild-type ADH subunit retains full enzyme activity [Hollocher and Place (1988) Genetics 116, 265-274]. Interestingly, the Ala159Thr mutant does not form either stable homodimers or heterodimers with wild-type ADH, suggesting that alanine-159 is important in stabilizing ADH dimers. The mutations were analysed in terms of a three-dimensional model of ADH using bacterial 20 beta-hydroxysteroid dehydrogenase and rat dihydropteridine reductase as templates. The model indicates that mutations in glycine-17 and glycine-93 affect the binding of NAD+. It also shows that alanine-159 is part of a hydrophobic anchor on the dimer interface of ADH. Replacement of alanine-159 with threonine, which has a larger side chain and can hydrogen bond with water, is likely to reduce the strength of the hydrophobic interaction. The three-dimensional model shows that glycine-184 is close to the substrate binding site. Replacement of glycine-184 with aspartic acid is likely to alter the position of threonine-186, which we propose hydrogen bonds to the carboxamide moiety of NAD+. Also, the negative charge on the aspartic acid side chain may interact with the substrate and/or residues in the substrate binding site. These mutations provide information about ADH catalysis and the stability of dimers, which may also be useful in understanding homologous dehydrogenases, which include the human 17 beta-hydroxysteroid, 11 beta-hydroxysteroid and 15-hydroxyprostaglandin dehydrogenases.

Three-Dimensional Solution Structure of Lactoferricin B, an Antimicrobial Peptide Derived from Bovine Lactoferrin†

Biochemistry ◽  
1998 ◽  
Vol 37 (12) ◽  
pp. 4288-4298 ◽  
Author(s):  
Peter M. Hwang ◽  
Ning Zhou ◽  
Xi Shan ◽  
Cheryl H. Arrowsmith ◽  
Hans J. Vogel
Keyword(s):  
Antimicrobial Peptide ◽  
Solution Structure ◽  
Three Dimensional ◽  
Bovine Lactoferrin ◽  
Dimensional Solution

Three-dimensional solution structure of the pleckstrin homology domain from dynamin

1994 ◽  
Vol 4 (10) ◽  
pp. 884-891 ◽  
Author(s):  
A.Kristina Downing ◽  
Paul C. Driscoll ◽  
Ivan Gout ◽  
Kamran Salim ◽  
Markéta J. Zvelebil ◽  
...  
Keyword(s):  
Solution Structure ◽  
Three Dimensional ◽  
Pleckstrin Homology Domain ◽  
Pleckstrin Homology ◽  
Dimensional Solution

The three-dimensional solution structure and dynamic properties of the human FADD death domain 1 1Edited by A. Fersht

2000 ◽  
Vol 302 (1) ◽  
pp. 171-188 ◽  
Author(s):  
Helena Berglund ◽  
Dionne Olerenshaw ◽  
Andrew Sankar ◽  
Matthias Federwisch ◽  
Neil Q McDonald ◽  
...  
Keyword(s):  
Solution Structure ◽  
Dynamic Properties ◽  
Three Dimensional ◽  
Death Domain ◽  
Dimensional Solution

The Three-Dimensional Solution Structure of the SH2 Domain from p55blkKinase

Biochemistry ◽  
1996 ◽  
Vol 35 (20) ◽  
pp. 6201-6211 ◽  
Author(s):  
William J. Metzler ◽  
Barbara Leiting ◽  
Kelly Pryor ◽  
Luciano Mueller ◽  
Bennett T. Farmer
Keyword(s):  
Solution Structure ◽  
Three Dimensional ◽  
Sh2 Domain ◽  
Dimensional Solution
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