کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
2048955 1074107 2010 5 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Solution structure of the N-terminal catalytic domain of human H-REV107 – A novel circular permutated NlpC/P60 domain
موضوعات مرتبط
علوم زیستی و بیوفناوری علوم کشاورزی و بیولوژیک دانش گیاه شناسی
پیش نمایش صفحه اول مقاله
Solution structure of the N-terminal catalytic domain of human H-REV107 – A novel circular permutated NlpC/P60 domain
چکیده انگلیسی

H-REV107 is a Ca2+-independent phospholipase A1/2, and it is also a pro-apoptosis protein belonging to the novel class II tumor suppressor family, H-REV107-like family. Here we report the solution structure of the N-terminal catalytic domain of human H-REV107, which has a similar architecture to classical NlpC/P60 domains, even though their fold topologies are different due to circular permutation in the primary sequence. The phospholipase active site possesses a structurally conserved Cys–His–His catalytic triad as found in NlpC/P60 peptidases, indicating H-REV107 should adopt a similar catalytic mechanism towards phospholipid substrates to that of NlpC/P60 peptidases towards peptides. As H-REV107 is highly similar to lecithin retinol acyltransferase, our study also provides structural insight to this essential enzyme in retinol metabolism.

ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: FEBS Letters - Volume 584, Issue 19, 8 October 2010, Pages 4222–4226
نویسندگان
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