2K51
NMR Solution Structure of the Neurotrypsin Kringle Domain
Summary for 2K51
| Entry DOI | 10.2210/pdb2k51/pdb |
| Related | 2K4R |
| Descriptor | Neurotrypsin (1 entity in total) |
| Functional Keywords | neurotrypsin, kringle domain, disulfide-rich protein fold, serine endopeptidase, hydrolase, extracellular proteolysis |
| Biological source | Rattus norvegicus (Rat) |
| Total number of polymer chains | 1 |
| Total formula weight | 8542.46 |
| Authors | Ozhogina, O.A. (deposition date: 2008-06-23, release date: 2008-12-09, Last modification date: 2024-10-16) |
| Primary citation | Ozhogina, O.A.,Grishaev, A.,Bominaar, E.L.,Llinas, M. NMR Solution Structure of the Neurotrypsin Kringle Domain Biochemistry, 47:12290-12298, 2008 Cited by PubMed 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. PubMed: 18956887DOI: 10.1021/bi800555z PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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