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The structure of vanin 1: a key enzyme linking metabolic disease and inflammation.
- Source :
-
Acta Crystallographica: Section D (Wiley-Blackwell) . Dec2014, Vol. 70 Issue 12, p3320-3329. 10p. - Publication Year :
- 2014
-
Abstract
- Although part of the coenzyme A pathway, vanin 1 (also known as pantetheinase) sits on the cell surface of many cell types as an ectoenzyme, catalyzing the breakdown of pantetheine to pantothenic acid (vitamin B5) and cysteamine, a strong reducing agent. Vanin 1 was initially discovered as a protein involved in the homing of leukocytes to the thymus. Numerous studies have shown that vanin 1 is involved in inflammation, and more recent studies have shown a key role in metabolic disease. Here, the X-ray crystal structure of human vanin 1 at 2.25 Å resolution is presented, which is the first reported structure from the vanin family, as well as a crystal structure of vanin 1 bound to a specific inhibitor. These structures illuminate how vanin 1 can mediate its biological roles by way of both enzymatic activity and protein-protein interactions. Furthermore, it sheds light on how the enzymatic activity is regulated by a novel allosteric mechanism at a domain interface. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 09074449
- Volume :
- 70
- Issue :
- 12
- Database :
- Academic Search Index
- Journal :
- Acta Crystallographica: Section D (Wiley-Blackwell)
- Publication Type :
- Academic Journal
- Accession number :
- 99840240
- Full Text :
- https://doi.org/10.1107/S1399004714022767