Publication Date:
2009-05-22
Description:
Transmembrane sodium-ion gradients provide energy that can be harnessed by 'secondary transporters' to drive the translocation of solute molecules into a cell. Decades of study have shown that such sodium-coupled transporters are involved in many physiological processes, making them targets for the treatment of numerous diseases. Within the past year, crystal structures of several sodium-coupled transporters from different families have been reported, showing a remarkable structural conservation between functionally unrelated transporters. These atomic-resolution structures are revealing the mechanism of the sodium-coupled transport of solutes across cellular membranes.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Krishnamurthy, Harini -- Piscitelli, Chayne L -- Gouaux, Eric -- Howard Hughes Medical Institute/ -- England -- Nature. 2009 May 21;459(7245):347-55. doi: 10.1038/nature08143.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Vollum Institute, Oregon Health and Science University, 3181 SW Sam Jackson Park Road, Oregon 97239, USA.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/19458710" target="_blank"〉PubMed〈/a〉
Keywords:
Animals
;
Binding Sites
;
Humans
;
Membrane Transport Proteins/*chemistry/*metabolism
;
Models, Molecular
;
Protein Conformation
;
Sodium/*metabolism
Print ISSN:
0028-0836
Electronic ISSN:
1476-4687
Topics:
Biology
,
Chemistry and Pharmacology
,
Medicine
,
Natural Sciences in General
,
Physics
