To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.
General Information
DRAVP ID DRAVPe01940
Peptide Name HRA1
Sequence TIRLESEVTAIKNALKKTNEAVSTLGNGVRVLATAVRELKDFV
Sequence Length 43
UniProt ID No entry found
Source Synthetic construct
Activity Information
Target Organism HMPV
Assay RT-PCR assay
Activity
Hemolytic Activity No hemolysis information or data found in the reference(s) presented in this entry
Cytotoxicity
Binding Target F protein
Mechanism In hMPV, the F proteins assemble as trimers inside which three HRA (as well as three HRB) are creating a coiled coil. Then, the two pairs of coiled-coils (HRA and HRB) interact, creating a six-helix bundle structure that brings the viral and the cellular membranes close together, causing membrane merge and fusion pore dilatation. Peptide designed based in the HRA and HRB domains of the F protein can inhibit the process.
Structure Information
PDB ID None
Predicted Structure Download No predicted structure available
Linear/Cyclic Linear
N-terminal Modification Free
C-terminal Modification Free
Other Modification None
Stereochemistry L
Physicochemical Information
Formula C204H353N59O64
Absent amino acids CHMPQWY
Common amino acids V
Mass 4656.4
Pl 9.52
Basic residues 7
Acidic residues 5
Hydrophobic residues 19
Net charge 2
Boman Index -6990
Hydrophobicity 4.65
Aliphatic Index 115.58
Half Life
Extinction Coefficient cystines 0
Absorbance 280nm 0
Polar residues 12
Literature Information
Literature 1
Title Identification and evaluation of a highly effective fusion inhibitor for human metapneumovirus.
Pubmed ID 17967906
Reference Antimicrob Agents Chemother. 2008 Jan;52(1):279-87.
Author Deffrasnes C, Hamelin ME, Prince GA, Boivin G.
To the extent possible under law, the person who associated CC0 with this work has waived all copyright and related or neighboring rights to this work.