کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
2049321 | 1074123 | 2010 | 9 صفحه PDF | دانلود رایگان |
![عکس صفحه اول مقاله: Structure and function of mitochondrial carriers – Role of the transmembrane helix P and G residues in the gating and transport mechanism Structure and function of mitochondrial carriers – Role of the transmembrane helix P and G residues in the gating and transport mechanism](/preview/png/2049321.png)
To date, 22 mitochondrial carrier subfamilies have been functionally identified based on substrate specificity. Structural, functional and bioinformatics studies have pointed to the existence in the mitochondrial carrier superfamily of a substrate-binding site in the internal carrier cavity, of two salt-bridge networks or gates that close the cavity alternatively on the matrix or the cytosolic side of the membrane, and of conserved prolines and glycines in the transmembrane α-helices. The significance of these properties in the structural changes occurring during the catalytic substrate translocation cycle are discussed within the context of a transport mechanism model. Most experimentally produced and disease-causing missense mutations concern carrier regions corresponding to the substrate-binding site, the two gates and the conserved prolines and glycines.
Journal: FEBS Letters - Volume 584, Issue 9, 3 May 2010, Pages 1931–1939