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 DRAVPe01941
Peptide Name HRA2
Sequence AKTIRLESEVTAIKNALKKTNEAVSTLGNGVRVLATAVRELKDFVSKN
Sequence Length 48
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 C226H393N67O71
Absent amino acids CHMPQWY
Common amino acids AKV
Mass 5185.01
Pl 9.99
Basic residues 9
Acidic residues 5
Hydrophobic residues 20
Net charge 4
Boman Index -8923
Hydrophobicity -17.29
Aliphatic Index 105.63
Half Life
Extinction Coefficient cystines 0
Absorbance 280nm 0
Polar residues 14
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.