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PDBsum entry 2k4r

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Hydrolase PDB id
2k4r
Contents
Protein chain
77 a.a.

References listed in PDB file
Key reference
Title Nmr solution structure of the neurotrypsin kringle domain.
Authors O.A.Ozhogina, A.Grishaev, E.L.Bominaar, L.Patthy, M.Trexler, M.Llinás.
Ref. Biochemistry, 2008, 47, 12290-12298.
PubMed id 18956887
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.
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