Helix-helix interactions in membrane domains of bitopic proteins: Specificity and role of lipid environment
Biochimica et Biophysica Acta (BBA) - Biomembranes, ISSN: 0005-2736, Vol: 1859, Issue: 4, Page: 561-576
2017
- 72Citations
- 103Captures
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Example: if you select the 1-year option for an article published in 2019 and a metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019. If you select the 3-year option for the same article published in 2019 and the metric category shows 90%, that means that the article or review is performing better than 90% of the other articles/reviews published in that journal in 2019, 2018 and 2017.
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Metrics Details
- Citations72
- Citation Indexes72
- 72
- CrossRef56
- Captures103
- Readers103
- 103
Review Description
Interaction between transmembrane helices often determines biological activity of membrane proteins. Bitopic proteins, a broad subclass of membrane proteins, form dimers containing two membrane-spanning helices. Some aspects of their structure-function relationship cannot be fully understood without considering the protein-lipid interaction, which can determine the protein conformational ensemble. Experimental and computer modeling data concerning transmembrane parts of bitopic proteins are reviewed in the present paper. They highlight the importance of lipid-protein interactions and resolve certain paradoxes in the behavior of such proteins. Besides, some properties of membrane organization provided a clue to understanding of allosteric interactions between distant parts of proteins. Interactions of these kinds appear to underlie a signaling mechanism, which could be widely employed in the functioning of many membrane proteins. Treatment of membrane proteins as parts of integrated fine-tuned proteolipid system promises new insights into biological function mechanisms and approaches to drug design. This article is part of a Special Issue entitled: Lipid order/lipid defects and lipid-control of protein activity edited by Dirk Schneider.
Bibliographic Details
http://www.sciencedirect.com/science/article/pii/S0005273616303704; http://dx.doi.org/10.1016/j.bbamem.2016.10.024; http://www.scopus.com/inward/record.url?partnerID=HzOxMe3b&scp=85007369942&origin=inward; http://www.ncbi.nlm.nih.gov/pubmed/27884807; https://linkinghub.elsevier.com/retrieve/pii/S0005273616303704; https://dx.doi.org/10.1016/j.bbamem.2016.10.024
Elsevier BV
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