Loading
PDBj
MenuPDBj@FacebookPDBj@X(formerly Twitter)PDBj@BlueSkyPDBj@YouTubewwPDB FoundationwwPDBDonate
RCSB PDBPDBeBMRBAdv. SearchSearch help

1TV0

Solution structure of cryptdin-4, the most potent alpha-defensin from mouse Paneth cells

Summary for 1TV0
Entry DOI10.2210/pdb1tv0/pdb
NMR InformationBMRB: 6264
DescriptorCryptdin-4 (1 entity in total)
Functional Keywordsbeta sheet, beta hairpin, antimicrobial protein
Biological sourceMus musculus (house mouse)
Cellular locationSecreted: P28311
Total number of polymer chains1
Total formula weight3771.61
Authors
Jing, W.,Hunter, H.N.,Tanabe, H.,Ouellette, A.J.,Vogel, H.J. (deposition date: 2004-06-25, release date: 2005-01-04, Last modification date: 2024-10-30)
Primary citationJing, W.,Hunter, H.N.,Tanabe, H.,Ouellette, A.J.,Vogel, H.J.
Solution Structure of Cryptdin-4, a Mouse Paneth Cell alpha-Defensin.
Biochemistry, 43:15759-15766, 2004
Cited by
PubMed Abstract: Mammalian defensins are abundant antimicrobial peptides that contribute to host defense. They are characterized by several conserved amino acids, including six invariant cysteine residues which form three intramolecular disulfide bonds and stabilize the tertiary structure. Cryptdin-4 (Crp4), a mouse alpha-defensin with potent in vitro bactericidal activity, has a primary structure distinct from all known alpha-defensins in that its polypeptide backbone uniquely lacks three residues between Cys(IV) and Cys(V). NMR diffusion experiments showed that Crp4 is monomeric in solution, and its three-dimensional solution structure, determined by two-dimensional proton NMR, consists of a triple-stranded antiparallel beta-sheet with the beta-strands joined to each other by a series of tight turns and a beta-hairpin. However, the overall beta-sheet content in Crp4 is lower than that of other alpha-defensin structures, while the shape and orientation of the Crp4 beta-hairpin also differ from those of other alpha-defensin structures. These structural characteristics combined with the high overall cationicity of Crp4 may contribute to its broad bactericidal spectrum and membrane disruptive activity.
PubMed: 15595831
DOI: 10.1021/bi048645p
PDB entries with the same primary citation
Experimental method
SOLUTION NMR
Structure validation

247947

PDB entries from 2026-01-21

PDB statisticsPDBj update infoContact PDBjnumon