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“Of particular interest” — in the opinion of structural biologists
"Of particular interest"in the opinion of structural biologists. Papers "of particular interest" selected, from the previous year's literature, by the authors of reviews in the section on Lipids in the August 1992 issue of Current Opinion in Structural Biology.
Lipidic pheromones selected by Peter E. A. Teal and James H. Tumlinson COWLEY JJ, BROOKSBANK BW: Human Exposure to Putative Pheromones and Changes in Aspects of Social Behaviour. J Steroid Biochem Mol Biol 1991, 39:647-659. The results of experiments in which men and women were exposed to synthetic human pheromones are discussed. Exposure of women to 50t-androst-16-en-3aol resulted in significantly more interactions with men whereas exposure to short-chain fatty acids had no effect. No significant changes were found among men exposed to either treatment. The paper provides a good overview of current knowledge about the actions of pheromones in humans. MOLLER-SCHWARZED, HOULIHANPW: Pheromonal Activity of Single Castoreum Constituents in Beaver, Castor canadensis. J Chem Ecol 1991, 17:715-734. A detailed account of the behavioral effects of the individual pheromone components of beaver castoreum is given. The results clearly define the function of 4ethylphenol, 1,2-dihydroxybenzene, acetophenone and 3-hydroxyacetophenone as marking pheromones, and indicate that adult males play a greater role in scent marking and responding to non-resident beavers than do females. MARCUSS,, CALDWELLGA, MILLERD, XUE C-B, NAIDERF, BECKERJM: Significance of C-terminal Cysteine Modifications to the Biological Activity of the Saccharomyces cerevisiae a-factor Mating Pheromone. Mol Cell Biol 1991, 11:3603-3612. The biological significance of both the S-famesyl group and methyl ester groups of the lipopeptide a-factor mating pheromone of the yeast S. cerevisiae is documented. The study also reports results of structure-activity relationships using analogs in which the famesyl or methyl ester groups were substituted by other functional groups. The results indicate that the hydrophobicity imparted by the functional groups is critical for biological activity.
Apolipoprotein structure: crystals and models selected by David Atkinson MARCEL YL, PROVOST PR, KOA H, RAFFAI E, DAC NV, FRUCHART J-C, RASSART E: The Epitopes of Apolipoprotein A-I Define Distinct Structural Domains Including a Mobile Middle Region. J Biol Cbem 1991, 266:3644-3653. A comprehensive examination of the epitopes expressed by apoA-I. The epitopes are mapped to the A-I amino acid sequence and analyzed in terms of a model for the secondary structure of the protein.
440
BREITER DR, KANOST MR, BENNING MM, WESENBERGG, LAWJH, WELTSMA, RAYME~rr I, HOLDENHM: Molecular Structure of an Apolipoprotein Determined at 2.5A Resolution. Biochemistry 1991, 30:603-608. A report of the X-ray crystal structure of apoLP-III from the locust. This structure provides a detailed molecular characterization of the amphipathic helix and the tertiary folding of the helices in the water-soluble form of the protein. WILSON C, WARDELLMR, WEISGRABERKH, MAHLEYRW, AGARD DAz Three Dimensional Structure of the LDL Receptor Binding Domain of Human Apolipoprotein E. Science 1991, 252:1817-1822. The detailed molecular structure of the amino-terminal domain of apoE3. Similar to the structure for apoLPIll, this structure provides a detailed molecular characterization of the folding of amphipathic helices in the water-soluble form of the protein. In addition, the structure provides the first visualization of the region of the protein involved in receptor interaction.
Role of lipids in membrane structures selected by Derek Marsh CLEVESA, MCGEET, BANKAmSV: Phospholipid Transfer Proteins: a Biological Debut. Trends Cell Biol 1991, 1:30-34. Proposals for the mechanism whereby the SEC14p (phosphatidylinositol-transfer) protein may activate secretion from the Golgi in yeast, and a review of the involvement of phospholipid-transfer proteins in phospholipid equilibration and in secretion. BAZZI MD, NELSESTUENGL: Extensive Segregation of Acidic Phospholipids in Membranes Induced by Protein Kinase C and Related Proteins. Biochemistry 1991, 30:7961-7969. The authors demonstrate the formation of anionic lipidrich domains upon activation by the Ca2+-dependent binding of protein kinase C to mixed lipid membranes. MITCHELL DC, STRAUME M, LITMAN BJ: Role of sn-l-saturated/sn-2-polyunsaturated Phospholipids in Control of Membrane Receptor Conformational Equilibration: Effects of Cholesterol and Acyl Chain Unsaturation on the Metarhodopsin I-Metarhodopsin II Equilibrium. Biochemistry 1992, 31:662-670. A demonstration of the pronounced effect of lipid chain polyunsaturation on the meta I-meta II equilibrium o f rhodopsin, and the modulation of this equilibration in a compensatory fashion by cholesterol and temperature. This paper also includes a discussion of the sn-1/sn-2 chain asymmetry in membrane lipids in general.
© 1992 Current Biology
Lipidic pheromones selected by Peter E. A. Teal and James H. Tumlinson COWLEY JJ, BROOKSBANK BW: Human Exposure to Putative Pheromones and Changes in Aspects of Social Behaviour. J Steroid Biochem Mol Biol 1991, 39:647-659. The results of experiments in which men and women were exposed to synthetic human pheromones are discussed. Exposure of women to 50t-androst-16-en-3aol resulted in significantly more interactions with men whereas exposure to short-chain fatty acids had no effect. No significant changes were found among men exposed to either treatment. The paper provides a good overview of current knowledge about the actions of pheromones in humans. MOLLER-SCHWARZED, HOULIHANPW: Pheromonal Activity of Single Castoreum Constituents in Beaver, Castor canadensis. J Chem Ecol 1991, 17:715-734. A detailed account of the behavioral effects of the individual pheromone components of beaver castoreum is given. The results clearly define the function of 4ethylphenol, 1,2-dihydroxybenzene, acetophenone and 3-hydroxyacetophenone as marking pheromones, and indicate that adult males play a greater role in scent marking and responding to non-resident beavers than do females. MARCUSS,, CALDWELLGA, MILLERD, XUE C-B, NAIDERF, BECKERJM: Significance of C-terminal Cysteine Modifications to the Biological Activity of the Saccharomyces cerevisiae a-factor Mating Pheromone. Mol Cell Biol 1991, 11:3603-3612. The biological significance of both the S-famesyl group and methyl ester groups of the lipopeptide a-factor mating pheromone of the yeast S. cerevisiae is documented. The study also reports results of structure-activity relationships using analogs in which the famesyl or methyl ester groups were substituted by other functional groups. The results indicate that the hydrophobicity imparted by the functional groups is critical for biological activity.
Apolipoprotein structure: crystals and models selected by David Atkinson MARCEL YL, PROVOST PR, KOA H, RAFFAI E, DAC NV, FRUCHART J-C, RASSART E: The Epitopes of Apolipoprotein A-I Define Distinct Structural Domains Including a Mobile Middle Region. J Biol Cbem 1991, 266:3644-3653. A comprehensive examination of the epitopes expressed by apoA-I. The epitopes are mapped to the A-I amino acid sequence and analyzed in terms of a model for the secondary structure of the protein.
440
BREITER DR, KANOST MR, BENNING MM, WESENBERGG, LAWJH, WELTSMA, RAYME~rr I, HOLDENHM: Molecular Structure of an Apolipoprotein Determined at 2.5A Resolution. Biochemistry 1991, 30:603-608. A report of the X-ray crystal structure of apoLP-III from the locust. This structure provides a detailed molecular characterization of the amphipathic helix and the tertiary folding of the helices in the water-soluble form of the protein. WILSON C, WARDELLMR, WEISGRABERKH, MAHLEYRW, AGARD DAz Three Dimensional Structure of the LDL Receptor Binding Domain of Human Apolipoprotein E. Science 1991, 252:1817-1822. The detailed molecular structure of the amino-terminal domain of apoE3. Similar to the structure for apoLPIll, this structure provides a detailed molecular characterization of the folding of amphipathic helices in the water-soluble form of the protein. In addition, the structure provides the first visualization of the region of the protein involved in receptor interaction.
Role of lipids in membrane structures selected by Derek Marsh CLEVESA, MCGEET, BANKAmSV: Phospholipid Transfer Proteins: a Biological Debut. Trends Cell Biol 1991, 1:30-34. Proposals for the mechanism whereby the SEC14p (phosphatidylinositol-transfer) protein may activate secretion from the Golgi in yeast, and a review of the involvement of phospholipid-transfer proteins in phospholipid equilibration and in secretion. BAZZI MD, NELSESTUENGL: Extensive Segregation of Acidic Phospholipids in Membranes Induced by Protein Kinase C and Related Proteins. Biochemistry 1991, 30:7961-7969. The authors demonstrate the formation of anionic lipidrich domains upon activation by the Ca2+-dependent binding of protein kinase C to mixed lipid membranes. MITCHELL DC, STRAUME M, LITMAN BJ: Role of sn-l-saturated/sn-2-polyunsaturated Phospholipids in Control of Membrane Receptor Conformational Equilibration: Effects of Cholesterol and Acyl Chain Unsaturation on the Metarhodopsin I-Metarhodopsin II Equilibrium. Biochemistry 1992, 31:662-670. A demonstration of the pronounced effect of lipid chain polyunsaturation on the meta I-meta II equilibrium o f rhodopsin, and the modulation of this equilibration in a compensatory fashion by cholesterol and temperature. This paper also includes a discussion of the sn-1/sn-2 chain asymmetry in membrane lipids in general.
© 1992 Current Biology