PMID- 23311880
OWN - NLM
STAT- MEDLINE
DCOM- 20130716
LR  - 20211021
IS  - 1520-5207 (Electronic)
IS  - 1520-6106 (Print)
IS  - 1520-5207 (Linking)
VI  - 117
IP  - 5
DP  - 2013 Feb 7
TI  - Organization and dynamics of the N-terminal domain of chemokine receptor CXCR1 in 
      reverse micelles: effect of graded hydration.
PG  - 1225-33
LID - 10.1021/jp3095352 [doi]
AB  - Water plays a fundamental role in the folding, structure, dynamics, and function 
      of proteins and peptides. The extracellular N-terminal domain of chemokine 
      receptors is crucial in mediating binding affinity, receptor selectivity, and 
      regulating function. The flexible N-terminal domain becomes ordered in membranes 
      and membrane-mimetic assemblies, thereby indicating that the membrane could play 
      an important role in regulating CXC chemokine receptor 1 (CXCR1) function. In 
      view of the role of hydration in lipid-protein interactions in membranes, we 
      explored the organization and dynamics of a 34-mer peptide of the CXCR1 
      N-terminal domain in reverse micelles by utilizing a combination of 
      fluorescence-based approaches and circular dichroism spectroscopy. Our results 
      show that the secondary structure adopted by the CXCR1 N-domain is critically 
      dependent on hydration. The tryptophan residues of the CXCR1 N-domain experience 
      motional restriction and exhibit red edge excitation shift (REES) upon 
      incorporation in reverse micelles. REES and fluorescence lifetime exhibit 
      reduction with increasing reverse micellar hydration. Time-resolved fluorescence 
      anisotropy measurements reveal the effect of hydration on peptide rotational 
      dynamics. Taken together, these results constitute the first report demonstrating 
      modulation in the organization and dynamics of the N-terminal domain of a 
      chemokine receptor in a membrane-like environment of varying hydration. We 
      envisage that these results are relevant in the context of hydration in the 
      function of G protein-coupled receptors.
FAU - Chaudhuri, Arunima
AU  - Chaudhuri A
AD  - Centre for Cellular and Molecular Biology, Council of Scientific and Industrial 
      Research, Uppal Road, Hyderabad 500 007, India.
FAU - Basu, Pritam
AU  - Basu P
FAU - Haldar, Sourav
AU  - Haldar S
FAU - Kombrabail, Mamata
AU  - Kombrabail M
FAU - Krishnamoorthy, G
AU  - Krishnamoorthy G
FAU - Rajarathnam, Krishna
AU  - Rajarathnam K
FAU - Chattopadhyay, Amitabha
AU  - Chattopadhyay A
LA  - eng
GR  - R01 AI069152/AI/NIAID NIH HHS/United States
GR  - R01-AI069152/AI/NIAID NIH HHS/United States
PT  - Journal Article
PT  - Research Support, N.I.H., Extramural
PT  - Research Support, Non-U.S. Gov't
DEP - 20130128
PL  - United States
TA  - J Phys Chem B
JT  - The journal of physical chemistry. B
JID - 101157530
RN  - 0 (Micelles)
RN  - 0 (Receptors, Interleukin-8A)
RN  - 059QF0KO0R (Water)
SB  - IM
MH  - Amino Acid Sequence
MH  - Fluorescence Polarization
MH  - *Micelles
MH  - Molecular Sequence Data
MH  - Protein Structure, Secondary
MH  - Protein Structure, Tertiary
MH  - Receptors, Interleukin-8A/*chemistry/*metabolism
MH  - Water/*chemistry
PMC - PMC3580202
MID - NIHMS438973
EDAT- 2013/01/15 06:00
MHDA- 2013/07/17 06:00
PMCR- 2014/02/07
CRDT- 2013/01/15 06:00
PHST- 2013/01/15 06:00 [entrez]
PHST- 2013/01/15 06:00 [pubmed]
PHST- 2013/07/17 06:00 [medline]
PHST- 2014/02/07 00:00 [pmc-release]
AID - 10.1021/jp3095352 [doi]
PST - ppublish
SO  - J Phys Chem B. 2013 Feb 7;117(5):1225-33. doi: 10.1021/jp3095352. Epub 2013 Jan 
      28.