TAILIEUCHUNG - Báo cáo khoa học: Intermodule cooperativity in the structure and dynamics of consecutive complement control modules in human C1r Structural biology

The modular C1r protein is the first protease activated in the classical complement pathway, a key component of innate immunity. Activation of the heteropentameric C1 complex, possibly accompanied by major inter-subunit re-arrangements besides proteolytic cleavage, requires targeted regulation of flexibility within the context of the intramolecular and inter-molecular interaction networks of the complex. | Intermodule cooperativity in the structure and dynamics of consecutive complement control modules in human C1r Structural biology 1 2 2 2 2 Andras Láng Katalin Szilagyi Balazs Major Peter Gal Peter Zavodszky and Andras Perczel1 3 1 Laboratory of StructuralChemistry and Biology Institute of Chemistry Eotvos Lorand University Pazmany Peter sétếsny 1 A Budapest Hungary 2 Institute of Enzymology BiologicalResearch Center Hungarian Academy of Sciences Budapest Hungary 3 Protein Modeling Group HAS-ELTE Institute of Chemistry Eotvos Lorand University Budapest Hungary Keywords cooperativity dynamics flexibility modularity NMR-spectroscopy Correspondence A. Perczel Institute of Chemistry Eotvos Lorand University H-1518 112 PO Box 32 Budapest Hungary Fax 36 1 372 2620 Tel 36 1 372 2600 E-mail perczel@ Website http These authors contributed equally to this work Received 26 May 2010 revised 22 June 2010 accepted 27 July 2010 doi The modular C1r protein is the first protease activated in the classical complement pathway a key component of innate immunity. Activation of the heteropentameric C1 complex possibly accompanied by major intersubunit re-arrangements besides proteolytic cleavage requires targeted regulation of flexibility within the context of the intramolecular and inter-molecular interaction networks of the complex. In this study we prepared the two complement control protein CCP modules CCP1 and CCP2 of C1r in their free form as well as their tandem-linked construct CCP1CCP2 to characterize their solution structure conformational dynamics and cooperativity. The structures derived from NMR signal dispersion and secondary chemical shifts were in good agreement with those obtained by X-ray crystallography. However successful heterologus expression of both the single CCP1 module and the CCP1CCP2 constructs required the attachment of the preceding N-terminal module CUB2 which could then be removed to .

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