PMID- 14581226
OWN - NLM
STAT- MEDLINE
DCOM- 20040713
LR  - 20191210
IS  - 0006-3495 (Print)
IS  - 1542-0086 (Electronic)
IS  - 0006-3495 (Linking)
VI  - 85
IP  - 5
DP  - 2003 Nov
TI  - TNP-AMP binding to the sarcoplasmic reticulum Ca(2+)-ATPase studied by infrared 
      spectroscopy.
PG  - 3262-70
AB  - Infrared spectroscopy was used to monitor the conformational change of 
      2',3'-O-(2,4,6-trinitrophenyl)adenosine 5'-monophosphate (TNP-AMP) binding to the 
      sarcoplasmic reticulum Ca(2+)-ATPase. TNP-AMP binding was observed in a 
      competition experiment: TNP-AMP is initially bound to the ATPase but is then 
      replaced by beta,gamma-iminoadenosine 5'-triphosphate (AMPPNP) after AMPPNP 
      release from P(3)-1-(2-nitrophenyl)ethyl AMPPNP (caged AMPPNP). The resulting 
      infrared difference spectra are compared to those of AMPPNP binding to the free 
      ATPase, to obtain a difference spectrum that reflects solely TNP-AMP binding to 
      the Ca(2+)-ATPase. TNP-AMP used as an ATP analog in the crystal structure of the 
      sarcoplasmic reticulum Ca(2+)-ATPase was found to induce a conformational change 
      upon binding to the ATPase. It binds with a binding mode that is different from 
      that of AMPPNP, ATP, and other tri- and diphosphate nucleotides: TNP-AMP binding 
      causes partially opposite and smaller conformational changes compared to ATP or 
      AMPPNP. The conformation of the TNP-AMP ATPase complex is more similar to that of 
      the E1Ca(2) state than to that of the E1ATPCa(2) state. Regarding the use of 
      infrared spectroscopy as a technique for ligand binding studies, our results show 
      that infrared spectroscopy is able to distinguish different binding modes.
FAU - Liu, Man
AU  - Liu M
AD  - Institut fur Biophysik, Johann Wolfgang Goethe-Universitat, Frankfurt am Main, 
      Germany.
FAU - Barth, Andreas
AU  - Barth A
LA  - eng
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Biophys J
JT  - Biophysical journal
JID - 0370626
RN  - 0 (Macromolecular Substances)
RN  - 415SHH325A (Adenosine Monophosphate)
RN  - 84430-16-0 (2',3'-O (2,4,6-trinitrocyclohexadienylidine)adenosine 
      5'-monophosphate)
RN  - EC 7.2.2.10 (Calcium-Transporting ATPases)
SB  - IM
MH  - Adenosine Monophosphate/*analogs & derivatives/*chemistry/metabolism
MH  - Binding Sites
MH  - Binding, Competitive
MH  - Calcium-Transporting ATPases/*chemistry/metabolism
MH  - Macromolecular Substances
MH  - Molecular Conformation
MH  - Protein Binding
MH  - Protein Conformation
MH  - Sarcoplasmic Reticulum/*chemistry/*enzymology/metabolism
MH  - Spectroscopy, Fourier Transform Infrared/*methods
PMC - PMC1303602
EDAT- 2003/10/29 05:00
MHDA- 2004/07/14 05:00
PMCR- 2004/11/01
CRDT- 2003/10/29 05:00
PHST- 2003/10/29 05:00 [pubmed]
PHST- 2004/07/14 05:00 [medline]
PHST- 2003/10/29 05:00 [entrez]
PHST- 2004/11/01 00:00 [pmc-release]
AID - S0006-3495(03)74744-4 [pii]
AID - 23366 [pii]
AID - 10.1016/S0006-3495(03)74744-4 [doi]
PST - ppublish
SO  - Biophys J. 2003 Nov;85(5):3262-70. doi: 10.1016/S0006-3495(03)74744-4.