کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
10757382 | 1050394 | 2014 | 6 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Peptides derived from human galectin-3 N-terminal tail interact with its carbohydrate recognition domain in a phosphorylation-dependent manner
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کلمات کلیدی
CRDHSQCnuclear magnetic resonance - رزونانس مغناطیسی هستهایAgglutinin - آگلوتیینNMR - تشدید مغناطیسی هستهای carbohydrate recognition domain - دامنه شناخت کربوهیدراتPhosphorylation - فسفریلاسیونPhosphopeptide - فسفوپپتیدLectin - لکتینCollagen - کلاژنGal-3 - گال سومGalectin-3 - گالکتین-3heteronuclear single-quantum coherence - یکپارچگی تک کوانتومی هترو هسته ای
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
Galectin-3 (Gal-3) is a multi-functional effector protein that functions in the cytoplasm and the nucleus, as well as extracellularly following non-classical secretion. Structurally, Gal-3 is unique among galectins with its carbohydrate recognition domain (CRD) attached to a rather long N-terminal tail composed mostly of collagen-like repeats (nine in the human protein) and terminating in a short non-collagenous terminal peptide sequence unique in this lectin family and not yet fully explored. Although several Ser and Tyr sites within the N-terminal tail can be phosphorylated, the physiological significance of this post-translational modification remains unclear. Here, we used a series of synthetic (phospho)peptides derived from the tail to assess phosphorylation-mediated interactions with 15N-labeled Gal-3 CRD. HSQC-derived chemical shift perturbations revealed selective interactions at the backface of the CRD that were attenuated by phosphorylation of Tyr 107 and Tyr 118, while phosphorylation of Ser 6 and Ser 12 was essential. Controls with sequence scrambling underscored inherent specificity. Our studies shed light on how phosphorylation of the N-terminal tail may impact on Gal-3 function and prompt further studies using phosphorylated full-length protein.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochemical and Biophysical Research Communications - Volume 443, Issue 1, 3 January 2014, Pages 126-131
Journal: Biochemical and Biophysical Research Communications - Volume 443, Issue 1, 3 January 2014, Pages 126-131
نویسندگان
M. Álvaro BerbÃs, Sabine André, F. Javier Cañada, Rüdiger Pipkorn, Hans Ippel, Kevin H. Mayo, Dieter Kübler, Hans-Joachim Gabius, Jesús Jiménez-Barbero,