کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
5917579 | 1570742 | 2009 | 7 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Binding site of C-reactive protein on M-ficolin
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کلمات کلیدی
FBGGlcNAcN-acetyl-d-glucosamineMBLFicolinMASPBrevibacillus choshinensiscollagen-like domainInnate immunity - ایمنی ذاتیFibrinogen-like domain - دامنه فیبریژن مانندcircular dichroism - رنگ تابی دورانیMannose binding lectin - لکتین اتصال دهنده مانوزC-reactive protein - پروتئین واکنشی سیCRP - پروتئین واکنشی سی یا سی. آر. پی Weak affinity chromatography - کروماتوگرافی ضعف ضعیفcol - کول
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شناسی مولکولی
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چکیده انگلیسی
The binding abilities of human C-reactive protein (CRP) with the C-terminal fibrinogen-like (FBG) domain and the full-length form of human M-ficolin were investigated by pull-down and zonal affinity chromatography analyses. Pull-down assays using an N-acetyl-d-glucosamine (GlcNAc)-agarose column demonstrated that CRP binds to the trimeric FBG domains, and that the GlcNAc-binding ability of the FBG domain is unaffected by CRP binding. Interestingly, the full-length M-ficolin, comprising the N-terminal collagen-like (COL) and C-terminal FBG domains, displayed lower affinity for CRP, and the monomeric FBG domain showed virtually no binding to CRP, as qualitatively judged by zonal affinity chromatography using a GlcNAc column. These results indicated that CRP binding requires the trimeric form of the FBG domain, and that the presence of the COL domain reduces the interaction between CRP and M-ficolin. In addition, pull-down assays using a histidine-tag affinity column demonstrated that neither the full-length M-ficolin nor the trimeric FBG domains, immobilized through their C-terminal histidine tags, showed any affinity for CRP, indicating that the CRP binding site is located near Ala326 at the C-terminus of M-ficolin, spatially close to a neck region (around Pro115) between the FBG and COL domains. From these findings, we concluded that CRP binding is enhanced by conformational bending at the neck region of M-ficolin, to avoid steric hindrance by the COL domain. Such a situation may be generated by oligomeric M-ficolin binding to surfaces with widely distributed ligands, such as pathogens.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Molecular Immunology - Volume 47, Issues 2â3, December 2009, Pages 215-221
Journal: Molecular Immunology - Volume 47, Issues 2â3, December 2009, Pages 215-221
نویسندگان
Michikazu Tanio, Kaori Wakamatsu, Toshiyuki Kohno,