2k51
From Proteopedia
NMR Solution Structure of the Neurotrypsin Kringle Domain
Structural highlights
FunctionNETR_RAT Plays a role in neuronal plasticity and the proteolytic action may subserve structural reorganizations associated with learning and memory operations. Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedNeurotrypsin 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 (13)C 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. NMR Solution Structure of the Neurotrypsin Kringle Domain.,Ozhogina OA, Grishaev A, Bominaar EL, Patthy L, Trexler M, Llinas M Biochemistry. 2008 Oct 29. PMID:18956887[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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