|
|
|
Primary Information | |
|---|---|
| BoMiProt ID | Bomi4263 |
| Protein Name | Beta-defensin 12 |
| Organism | Bos taurus |
| Uniprot ID | P46170 |
| Milk Fraction | Whey |
| Aminoacid Length | 38 |
| Molecular Weight | 4106 |
| FASTA Sequence | Download |
| Gene Name | DEFB12 |
| Protein Existence Status | Reviewed |
Secondary Information | |
| Protein Function | Has bactericidal activity. Active against E.coli ML35 and S.aureus 502A. |
| Biochemical Properties | The N-terminal beta-strand and three locally well-defined tight turns form a hydrophobic face. Conserved isoleucine and glycine residues form a beta-bulge structure which initiates a beta-hairpin secondary structure motif composed of the second and C-terminal beta-strands. The beta-hairpin contains numerous charged residues and forms the cationic face of BNBD-12. The N-terminal residues were found to be disordered. The triple-stranded beta-sheet, the beta-bulge preceding the hairpin, and the cationic/hydrophobic amphiphilic character are definitive features of all defensin structures determined to date. |
| Site(s) of PTM(s) N-glycosylation, O-glycosylation, Phosphorylation | na |
| SCOP | Class : Small proteins Fold : Defensin-like Superfamily : Defensin-like Family : Defensin Domain Name : 1BNB A:1-38 |
| CATH | Matched CATH superfamily n/a |
| Predicted Disorder Regions | (11-28) |
| DisProt Annotation | |
| TM Helix Prediction | No TM helices |
| PDB ID | 1BNB, |
| Bibliography | 1.Zimmermann GR, Legault P, Selsted ME, Pardi A. Solution structure of bovine neutrophil beta-defensin-12: the peptide fold of the beta-defensins is identical to that of the classical defensins. Biochemistry. 1995 Oct 17;34(41):13663-71. doi: 10.1021/bi00041a048. PMID: 7577957. |