کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1979642 | 1061692 | 2007 | 9 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Protein–protein interactions regulate Ubl conjugation
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موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
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چکیده انگلیسی
The ubiquitin-like proteins (Ubls) can be covalently linked to target proteins to provide a critical signal in diverse cellular processes. Members of the Ubl family include ubiquitin itself and a growing number of homologs such as SUMO, Nedd8, ISG15 and Atg8. The enzymatic mechanism of Ubl conjugation involves an E1, E2, E3 cascade of enzymes that is well conserved between the Ubls. In the past two years, novel structural details of Ubl conjugation were uncovered through analysis of protein–protein complexes. This has given insight in activation of E1, the role of the target lysine in E2-dependent catalysis, the role of noncovalent Ubl binding in Ubl chain formation and the importance of dimerization of Ring-type E3 ligases.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Current Opinion in Structural Biology - Volume 17, Issue 6, December 2007, Pages 665–673
Journal: Current Opinion in Structural Biology - Volume 17, Issue 6, December 2007, Pages 665–673
نویسندگان
Puck Knipscheer, Titia K Sixma,