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Accueil > Publications > Recherche par années > Années 1990 > 1999

Roussel, A ; Spinelli, S ; Deret, S ; Navaza, J ; Aucouturier, P ; Cambillau, C

The structure of an entire noncovalent immunoglobulin kappa light-chain dimer (Bence-Jones protein) reveals a weak and unusual constant domains association

European Journal of Biochemistry 260 (1) 192-199

par Administrateur - publié le

Abstract :

Monoclonal free light chains secreted in immunoproliferative disorders art : frequently involved in renal complications, including a specific proximal tubule impairment, Fanconi’s syndrome. The latter is characterized in most cases by intracellular crystallization including a light-chain variable-domain fragment which resists lysosomal proteases. Bence-Jones protein (BJP) DEL was isolated from a patient with myeloma-associated Fanconi’s syndrome. The crystal structure of this human K immunoglobulin light-chain noncovalent dimer was determined using molecular replacement with the structure of molecule REI, as the variable domain, and that of BJP LOC as the constant domain.