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| Content Provider | Springer Nature Link |
|---|---|
| Author | Dhani, Sonja U. Bear, Christine E. |
| Copyright Year | 2005 |
| Abstract | The ClC family of chloride channels and transporters includes several members in which mutations have been associated with human disease. Clearly, an understanding of the structure–function relationships of these proteins will be critical in defining the molecular mechanisms underlying disease pathogenesis. The X-ray crystal structure of prokaryotic ClC proteins provides an exquisite template with which to model molecular aspects of eukaryotic ClC protein function. The dimeric structure of these proteins highlights the pivotal importance of intermolecular interactions in the modulation of channel/transporter activity, while mutagenesis studies implicate a crucial role for intrinsic interdomain interactions in regulated function. In this review, we will initially focus on the channel forming members of this family and discuss interactions within homodimeric channel complexes important for gating. Finally, with regard to both channel and transporter family members, we will discuss the multiple heteromeric interactions which occur with cytosolic proteins, and the putative functional impact of these interactions. |
| Starting Page | 708 |
| Ending Page | 715 |
| Page Count | 8 |
| File Format | |
| ISSN | 00316768 |
| Journal | Pflügers Archiv |
| Volume Number | 451 |
| Issue Number | 6 |
| e-ISSN | 14322013 |
| Language | English |
| Publisher | Springer-Verlag |
| Publisher Date | 2005-09-16 |
| Publisher Place | Berlin, Heidelberg |
| Access Restriction | One Nation One Subscription (ONOS) |
| Subject Keyword | Dimeric interface Domain–domain interaction Channel gating Post-translational modification Regulated trafficking |
| Content Type | Text |
| Resource Type | Article |
| Subject | Physiology Physiology (medical) Clinical Biochemistry |
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