Protein : DEFB2
Description : Defensin beta 2
Skin-antimicrobial peptide 1
HBD-2 was first isolated from inflamed skin of patients with psoriasis.
Family : Vertebrate Beta
Organism : Homo sapiens (Human)
Alias
SAP1
HBD2
HBD-2
DEFB-2
DEFB102
BD-2
DEFB102
Other Databases
NCBI: 1673
SwissProt: O15263
HGNG: 2767
OMIM: 602215
Expression
Sites of Expression : Skin, lung, trachea, keratinocytes, gingival mucosa, skin and epithelia of the airway system, mucosal surfaces of the respiratory track, oral cavity and intestine, placenta
HBD2 expression is induced in response to inflammation in all epithelia tested (PMID:11516756). The expression of HBD-2 is locally regulated by inflammation. HBD-2 mRNA is markedly increased in the epidermis surrounding inflamed regions, but not detectable in adjacent non-inflamed areas (PMID:9831658). HBD-2 is upregulated by microorganisms or tumor necrosis factor-alpha (TNF-alpha).
Sequence Information
Description:Defensin, beta 2 precursor
Sequence Length:64 aa
Protein Sequence:MRVLYLLFSF LFIFLMPLPG VFGGIGDPVT CLKSGAICHP VFCPRRYKQI GTCGLPGTKC CKKP
Molecular Weight:7038 Da
Sequence Organization:Signal peptide: 1-23
Mature peptide: 24-64
Organisation of Gene
Chromosome Location:8p22-p23.1
Description:GenBank Accession number: AF040153
The HBD-2 gene spanned about 2 kb with two exons and one intron. HBD-2 intron spans 1610bp. The first 81bp exon encodes the signal sequence and the second 238bp exon encodes the mature HBD-2 and a very short segment of the propeptide
A TATA box sequence CTTTATAAGGTGGAA is located at position -45bp relative to the first cDNA base, and four NF-kB binding sites are found at positions -2209bp, -208bp, 1626bp and 2332bp. [PMID:9831658]
Unlike HBD-1, the HBD-2 gene contains several binding sites for nuclear factor kappaB (NF-kB) which is implicated in transcriptional responses to lipopolysaccharide and pro-inflammatory cytokines.
Structure Information
Mature peptide Sequence:GIGDPVT CLKSGAICHP VFCPRRYKQI GTCGLPGTKC CKKP
Mature Sequence Length:41 aa
Net Charge:7
No. of disulfide bonds:3
Disulfide Connectivities:31-60, 38-53, 43-61
Structure:Both alpha-helix and beta-structure
Structure Description:HBD-2 monomer has a central, three-stranded beta-sheet fold similar to the alpha-defensins, as well as a small alpha-helix at the N terminus.
Experimental Evidence
Experimental System Used:NMR
Protein:1FQQ_A Protein chain A
Sequence:xigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
No. of Chains:1
All Other Databases:PDB: 1FQQ [ JMol | Astex Viewer ]
MMDB: 16324
 
Experimental System Used:NMR
Protein:1E4Q_A Protein chain A
Sequence:xvtclksgai chpvfcprry kqigtcglpg tkcckkp (37aa)
No. of Chains:1
All Other Databases:PDB: 1E4Q [ JMol | Astex Viewer ]
MMDB: 18211
 
Experimental System Used:X-Ray crystallography
Protein:1FD3_A Protein chain A
Sequence:gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD3_B Protein chain B
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD3_C Protein chain C
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD3_D Protein chain D
Sequence:gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
No. of Chains:4
All Other Databases:PDB: 1FD3 [ JMol | Astex Viewer ]
MMDB: 14724
 
Experimental System Used:X-Ray crystallography
Protein:1FD4_A Protein chain A
Sequence:gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_B Protein chain B
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_C Protein chain C
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_D Protein chain D
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_E Protein chain E
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_F Protein chain F
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_G Protein chain G
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_H Protein chain H
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_I Protein chain I
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_J Protein chain J
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_K Protein chain K
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_L Protein chain L
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_M Protein chain M
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_N Protein chain N
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_O Protein chain O
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
1FD4_P Protein chain P
Sequence: gigdpvtclk sgaichpvfc prrykqigtc glpgtkcckk p (41aa)
No. of Chains:16
All Other Databases:PDB: 1FD4 [ JMol | Astex Viewer ]
MMDB: 14725
Antimicrobial Activity
Microbe Type Microbe Name Antimicrobial Activity
FungusCandida albicans
Gram-negative bacteriaEscherichia coli
Gram-negative bacteriaPseudomonas aeruginosa
Gram-positive bacteriaStaphylococcus aureus
Literature
(1) Hoover DM, Rajashankar KR, Blumenthal R, Puri A, Oppenheim JJ, Chertov O, Lubkowski J. The structure of human beta-defensin-2 shows evidence of higher order oligomerization. J. Biol. Chem. 2000 Oct;275 (42):32911-8 [PMID: 10906336 ]
 
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