کد مقاله کد نشریه سال انتشار مقاله انگلیسی نسخه تمام متن
8455505 1548023 2014 8 صفحه PDF دانلود رایگان
عنوان انگلیسی مقاله ISI
Structural elucidation of full-length nidogen and the laminin-nidogen complex in solution
ترجمه فارسی عنوان
توضیح ساختاری کامل نیدوژن و لامینین-نیدوژن در محلول
کلمات کلیدی
پراکندگی نور پویا، پروتئین ماتریکس غیر سلولی، هیدرودینامیک، لامینین، نیدوژن-1، پراکندگی اشعه ایکس زاویه کوچک،
موضوعات مرتبط
علوم زیستی و بیوفناوری بیوشیمی، ژنتیک و زیست شناسی مولکولی تحقیقات سرطان
چکیده انگلیسی
Nidogen-1 is a key basement membrane protein that is required for many biological activities. It is one of the central elements in organizing basal laminae including those in the skin, muscle, and the nervous system. The self-assembling extracellular matrix that also incorporates fibulins, fibronectin and integrins is clamped together by networks formed between nidogen, perlecan, laminin and collagen IV. To date, the full-length version of nidogen-1 has not been studied in detail in terms of its solution conformation and shape because of its susceptibility to proteolysis. In the current study, we have expressed and purified full-length nidogen-1 and have investigated its solution behavior using size-exclusion chromatography (SEC), dynamic light scattering (DLS) and small angle X-ray scattering (SAXS). The ab initio shape reconstruction of the complex between nidogen-1 and the laminin γ-1 short arm confirms that the interaction is mediated solely by the C-terminal domains: the rest of the domains of both proteins do not participate in complex formation.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Matrix Biology - Volume 33, January 2014, Pages 60-67
نویسندگان
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