|Name:||Antibacterial protein LL-37|
Cleavage product 2 of Cathelicidin antimicrobial peptide
| First appeared in release:||Release 2.0 (02/14/2005)|
|SwissProt: ||CAMP_HUMAN |
|TrEMBL: || |
|NCBI (GI): ||1706745 |
|Source organism:||Homo sapiens (Human)|
10 20 30 40 50 60
| | | | | |
LLGDFFRKSK EKIGKEFKRI VQRIKDFLRN LVPRTES
|Functional narrative |
Human cathelicidin peptide with antibacterial properties. Antibacterial protein LL-37 is a cleavage product of Cathelicidin antimicrobial peptide (DP00004), comprised of aa residues 134-170 of the polyprotein.
|Map of ordered and disordered regions|
Note: 'Mouse' over a region to see the start and stop residues. Click on a region to see detailed information.
|Type:||Disordered - Extended|
|Location:||1 - 37|
|Modification type: ||Engineered |
|PDB: || |
|Structural/functional type: ||Function arises via a disorder to order transition |
|Functional classes: ||Unknown |
|Functional subclasses: ||Unknown |
|Detection methods: |
- Circular dichroism (CD) spectroscopy, near-UV (298 K; pH: 6; magnesium sulfate (salt) 84 mM; sodium chloride (salt) 160 mM)
- Johansson J, Gudmundsson GH, Rottenberg ME, Berndt KD, Agerberth B. "Conformation-dependent antibacterial activity of the naturally occurring human peptide LL-37." J Biol Chem. 1998; 273(6): 3718-24. PubMed: 9452503
The disordered region became significantly more disordered below pH 5. At pH of 2, it was completely disordered. At pH of 13, it adopted a helical structure.
Previous entry DP00004 has been split into polyprotein DP00004 and cleavage product
DP00004_C002. Disorder is characterized on the cleavage product.
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