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Rhodopsin TM6 Can Interact with Two Separate and Distinct Sites on Arrestin: Evidence for Structural Plasticity and Multiple Docking Modes in Arrestin–Rhodopsin Binding
[Image: see text] Various studies have implicated the concave surface of arrestin in the binding of the cytosolic surface of rhodopsin. However, specific sites of contact between the two proteins have not previously been defined in detail. Here, we report that arrestin shares part of the same bindin...
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| Main Authors: | , , , , |
|---|---|
| Formáid: | Artigo |
| Teanga: | Inglês |
| Foilsithe: |
American
Chemical Society
2014
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| Rochtain Ar Líne: | https://ncbi.nlm.nih.gov/pmc/articles/PMC4039336/ https://ncbi.nlm.nih.gov/pubmed/24724832 https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1021/bi401534y |
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