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PDBsum entry 2k4r
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References listed in PDB file
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Key reference
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Title
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Nmr solution structure of the neurotrypsin kringle domain.
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Authors
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O.A.Ozhogina,
A.Grishaev,
E.L.Bominaar,
L.Patthy,
M.Trexler,
M.Llinás.
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Ref.
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Biochemistry, 2008,
47,
12290-12298.
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PubMed id
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Abstract
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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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