| General information | | DisProt: | DP00004_C002 | | Name: | Antibacterial protein LL-37 | | Synonym(s): | CAMP_HUMAN
Cleavage product 2 of Cathelicidin antimicrobial peptide
| | First appeared in release: | Release 2.0 (02/14/2005) | | UniProt: | P49913 | | UniGene: | Hs.51120 | | SwissProt: | CAMP_HUMAN | | TrEMBL: | | | NCBI (GI): | 1706745 | | Source organism: | Homo sapiens (Human) | | Sequence length: | 37 | | Percent disordered: | 100% | | Homologues: | |
| Native sequence |
10 20 30 40 50 60
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LLGDFFRKSK EKIGKEFKRI VQRIKDFLRN LVPRTES
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| 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.
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| 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.
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| Region 1 | | Type: | Disordered - Extended | | Name: | | | Location: | 1 - 37 | | Length: | 37 | | Region sequence: |
LLGDFFRKSKEKIGKEFKRIVQRIKDFLRNLVPRTES | | 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)
| References:
- 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
| Comments: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.
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| Comments |
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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