التفاصيل البيبلوغرافية
| العنوان: |
The solution structure of the transducin‐α–uncoordinated 119 protein complex suggests occlusion of the Gβ 1 γ 1 ‐binding sites |
| المؤلفون: |
Cheguru, Pallavi, Majumder, Anurima, Yadav, Ravi, Gopalakrishna, Kota N., Gakhar, Lokesh, Artemyev, Nikolai O. |
| المساهمون: |
National Institutes of Health |
| المصدر: |
The FEBS Journal ; volume 282, issue 3, page 550-561 ; ISSN 1742-464X 1742-4658 |
| بيانات النشر: |
Wiley |
| سنة النشر: |
2014 |
| المجموعة: |
Wiley Online Library (Open Access Articles via Crossref) |
| الوصف: |
Uncoordinated 119 protein ( UNC 119) is a partner of transducin‐α subunit (Gα t ) that is essential for transducin trafficking in rod photoreceptors. The interaction is known to involve binding of the acylated N terminus of Gα t to the hydrophobic pocket of UNC 119. To gain insights into the mechanism of transducin trafficking, we isolated a highly pure protein complex between myristoylated chimeric Gα t (Gα t *) and UNC 119 50–240 , and examined the solution structure by small angle X‐ray scattering and chemical crosslinking. The solution structure of the Gα t – UNC 119 50–240 complex was derived with rigid body/ ab initio modeling against the small angle X‐ray scattering data by use of known atomic structures of Gα t and UNC 119, and a distance constraint based on the protein crosslinking with p ‐phenyldimaleimide. The model of the Gα t – UNC 119 50–240 complex indicates rotation and bending of the N‐terminal α‐helix of Gα t from its position in the structure of the heterotrimeric G‐protein transducin (G t ). This allows a considerably more compact complex conformation, which also suggests a novel interface involving the switch II /α3–β5 surface of Gα t . Supporting a novel interface, UNC 119 was found to bind full‐length Gα t * more strongly than the Gα t N‐terminal peptide. Furthermore, UNC 119 competed with the effector molecule phosphodiesterase‐6 γ‐subunit, which is known to bind to the same surface of Gα t . The solution structure of the Gα t – UNC 119 complex suggests that the ability of UNC 119 to dissociate G t subunits and release Gα t from the membrane is attributable to disruption and sterical occlusion of the Gβ 1 γ 1 ‐binding sites on Gα t . |
| نوع الوثيقة: |
article in journal/newspaper |
| اللغة: |
English |
| DOI: |
10.1111/febs.13161 |
| الإتاحة: |
https://doi.org/10.1111/febs.13161Test |
| حقوق: |
http://onlinelibrary.wiley.com/termsAndConditions#vorTest |
| رقم الانضمام: |
edsbas.43E554F7 |
| قاعدة البيانات: |
BASE |
