From Wikipedia, the free encyclopedia
In
molecular biology, the HAMP domain (present in
Histidine kinases,
Adenylate cyclases,
Methyl accepting proteins and
Phosphatases)
[1] is an approximately 50-amino acid
alpha-helical region that forms a dimeric, four-helical
coiled coil.
[2] It is found in bacterial sensor and
chemotaxis proteins and in eukaryotic
histidine kinases. The bacterial proteins are usually
integral membrane proteins and part of a
two-component signal transduction pathway. One or several copies of the HAMP domain can be found in association with other domains, such as the histidine kinase domain, the bacterial chemotaxis sensory transducer domain, the
PAS repeat, the
EAL domain, the
GGDEF domain, the protein
phosphatase 2C-like domain, the
guanylate cyclase domain, or the response
regulatory domain.
[3] In its most common setting, the HAMP domain transmits
conformational changes in periplasmic
ligand-binding
domains to
cytoplasmic
signalling kinase and methyl-acceptor domains and thus regulates the
phosphorylation or
methylation activity of homodimeric
receptors.
References
-
^ Aravind L, Ponting CP (July 1999).
"The cytoplasmic helical linker domain of receptor histidine kinase and methyl-accepting proteins is common to many prokaryotic signalling proteins". FEMS Microbiology Letters. 176 (1): 111–6.
doi:
10.1016/s0378-1097(99)00197-4.
PMID
10418137.
-
^ Hulko M, Berndt F, Gruber M, Linder JU, Truffault V, Schultz A, Martin J, Schultz JE, Lupas AN, Coles M (September 2006).
"The HAMP domain structure implies helix rotation in transmembrane signaling". Cell. 126 (5): 929–40.
doi:
10.1016/j.cell.2006.06.058.
PMID
16959572.
S2CID
18396561.
-
^ Dunin-Horkawicz S, Lupas AN (April 2010). "Comprehensive analysis of HAMP domains: implications for transmembrane signal transduction". Journal of Molecular Biology. 397 (5): 1156–74.
doi:
10.1016/j.jmb.2010.02.031.
PMID
20184894.