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Structures of Two Melanoma-Associated Antigens Suggest Allosteric Regulation of Effector Binding.

التفاصيل البيبلوغرافية
العنوان: Structures of Two Melanoma-Associated Antigens Suggest Allosteric Regulation of Effector Binding.
المؤلفون: Joseph A Newman, Christopher D O Cooper, Anette K Roos, Hazel Aitkenhead, Udo C T Oppermann, Hearn J Cho, Roman Osman, Opher Gileadi
المصدر: PLoS ONE, Vol 11, Iss 2, p e0148762 (2016)
بيانات النشر: Public Library of Science (PLoS), 2016.
سنة النشر: 2016
المجموعة: LCC:Medicine
LCC:Science
مصطلحات موضوعية: Medicine, Science
الوصف: The MAGE (melanoma associated antigen) protein family are tumour-associated proteins normally present only in reproductive tissues such as germ cells of the testis. The human genome encodes over 60 MAGE genes of which one class (containing MAGE-A3 and MAGE-A4) are exclusively expressed in tumours, making them an attractive target for the development of targeted and immunotherapeutic cancer treatments. Some MAGE proteins are thought to play an active role in driving cancer, modulating the activity of E3 ubiquitin ligases on targets related to apoptosis. Here we determined the crystal structures of MAGE-A3 and MAGE-A4. Both proteins crystallized with a terminal peptide bound in a deep cleft between two tandem-arranged winged helix domains. MAGE-A3 (but not MAGE-A4), is predominantly dimeric in solution. Comparison of MAGE-A3 and MAGE-A3 with a structure of an effector-bound MAGE-G1 suggests that a major conformational rearrangement is required for binding, and that this conformational plasticity may be targeted by allosteric binders.
نوع الوثيقة: article
وصف الملف: electronic resource
اللغة: English
تدمد: 1932-6203
Relation: http://europepmc.org/articles/PMC4766014?pdf=render; https://doaj.org/toc/1932-6203
DOI: 10.1371/journal.pone.0148762
URL الوصول: https://doaj.org/article/44063d5312b248f0a13c8fa7257d4839
رقم الأكسشن: edsdoj.44063d5312b248f0a13c8fa7257d4839
قاعدة البيانات: Directory of Open Access Journals
الوصف
تدمد:19326203
DOI:10.1371/journal.pone.0148762