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Hydrolase PDB id
2k51
Jmol
Contents
Protein chain
77 a.a. *
* Residue conservation analysis
PDB id:
2k51
Name: Hydrolase
Title: Nmr solution structure of the neurotrypsin kringle domain
Structure: Neurotrypsin. Chain: a. Fragment: kringle domain, nt/k, sequence database residues 84-160. Engineered: yes. Other_details: formula mass: 8533 da (natural abundance), 8635 da (15n-enriched), extinction coefficient (280 nm): 30855 m-1cm-1
Source: Rattus norvegicus. Rat. Organism_taxid: 10116. Gene: prss12, nt. Expressed in: escherichia coli. Expression_system_taxid: 562.
NMR struc: 1 models
Authors: O.A.Ozhogina
Key ref: O.A.Ozhogina et al. (2008). NMR Solution Structure of the Neurotrypsin Kringle Domain. Biochemistry, 47, 12290-12298. PubMed id: 18956887 DOI: 10.1021/bi800555z
Date:
23-Jun-08     Release date:   09-Dec-08    
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 Headers
 References

Protein chain
Pfam   ArchSchema ?
Q99JC8  (Q99JC8_RAT) -  Neurotrypsin
Seq:
Struc: 		 
Seq:
Struc: 		761 a.a.
77 a.a.
Key:    PfamA domain  PfamB domain  Secondary structure

 

 
DOI no: 10.1021/bi800555z Biochemistry 47:12290-12298 (2008)
PubMed id: 18956887  
 
 
NMR Solution Structure of the Neurotrypsin Kringle Domain.
O.A.Ozhogina, A.Grishaev, E.L.Bominaar, L.Patthy, M.Trexler, M.Llinás.
 
  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 (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.
 

Literature references that cite this PDB file's key reference

  PubMed id Reference
19524679 O.A.Ozhogina, and E.L.Bominaar (2009).
Characterization of the kringle fold and identification of a ubiquitous new class of disulfide rotamers.
  J Struct Biol, 168, 223-233.  
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