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¹H, ¹³C and ¹5N resonance assignments for the fibrillin-1 EGF2-EGF3-hybrid1-cbEGF1 four-domain fragment.
Robertson, Ian B; Osuch, Isabelle; Yadin, David A; Handford, Penny A; Jensen, Sacha A; Redfield, Christina.
Afiliação
  • Robertson IB; Department of Biochemistry, University of Oxford, South Parks Road, Oxford, OX1 3QU, UK.
Biomol NMR Assign ; 8(1): 189-94, 2014 Apr.
Article em En | MEDLINE | ID: mdl-23649688
Fibrillins are large extracellular glycoproteins that form the principal component of microfibrils. These perform a vital structural function in the extracellular matrix of many tissues. Fibrillins have also been implicated in mediating a number of protein-protein interactions, some of which may be significant in regulating growth factors such as transforming growth factor ß. Here we present the backbone and side-chain (1)H, (13)C and (15)N assignments for a 19 kDa protein fragment derived from the N-terminus of human fibrillin-1, encompassing four domains in total. These domains include the second and third epidermal growth factor-like (EGF) domains, the first hybrid domain (hyb1), and the first calcium-binding EGF domain of fibrillin-1. This region of fibrillin-1 is of particular interest as the hyb1 domain has been suggested to play a role in microfibril assembly, as well as several other protein-protein interactions.
Assuntos

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Cálcio / Ressonância Magnética Nuclear Biomolecular / Fator de Crescimento Epidérmico / Proteínas dos Microfilamentos Idioma: En Ano de publicação: 2014 Tipo de documento: Article

Texto completo: 1 Base de dados: MEDLINE Assunto principal: Cálcio / Ressonância Magnética Nuclear Biomolecular / Fator de Crescimento Epidérmico / Proteínas dos Microfilamentos Idioma: En Ano de publicação: 2014 Tipo de documento: Article