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NMR solution structure of the neurotrypsin Kringle domain.

ABSTRACT: Neurotrypsin is a multidomain protein that serves as a brain-specific serine protease. Here we report the NMR structure of its kringle domain, NT/K. The data analysis was performed with the BACUS (Bayesian analysis of coupled unassigned spins) algorithm. This study presents the first application of BACUS to the structure determination of a 13C unenriched protein for which no prior experimental 3D structure was available. NT/K adopts the kringle fold, consisting of an antiparallel beta-sheet bridged by an overlapping pair of disulfides. The structure reveals the presence of a surface-exposed left-handed polyproline II helix that is closely packed to the core beta-structure. This feature distinguishes NT/K from other members of the kringle fold and points toward a novel functional role for a kringle domain. Functional divergence among kringle domains is discussed on the basis of their surface and electrostatic characteristics.

SUBMITTER: Ozhogina OA

PROVIDER: S-EPMC2647577 | biostudies-literature | 2008 Nov

REPOSITORIES: biostudies-literature

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NMR solution structure of the neurotrypsin Kringle domain.

Ozhogina Olga A OA Grishaev Alexander A Bominaar Emile L EL Patthy László L Trexler Maria M Llinás Miguel M

Biochemistry 20081101 47

Neurotrypsin is a multidomain protein that serves as a brain-specific serine protease. Here we report the NMR structure of its kringle domain, NT/K. The data analysis was performed with the BACUS (Bayesian analysis of coupled unassigned spins) algorithm. This study presents the first application of BACUS to the structure determination of a 13C unenriched protein for which no prior experimental 3D structure was available. NT/K adopts the kringle fold, consisting of an antiparallel beta-sheet brid ...[more]

PMID: 18956887

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