The nature of the low-frequency normal modes of the E1Ca form of the SERCA1 Ca2+-ATPase

Annals of the New York Academy of Sciences

Volumn 986, Issue , 2003, Pages 344-346

  Reuter, N ^a   Hinsen, K ^b   Lacapere J J ^a  

^a INSERM   (France)

^b CENTRE DE BIOPHYSIQUE MOLÉCULAIRE   (France)

Author keywords

Ca2+ ATPase; Conformationai changes; Molecular modeling; Normal modes

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM);

ACTIVE TRANSPORT; BINDING SITE; CALCIUM BINDING; CALCIUM TRANSPORT; CALCULATION; CONFERENCE PAPER; CONFORMATIONAL TRANSITION; ENZYME CONFORMATION; ENZYME STRUCTURE; HYDROLYSIS; PROTEIN DOMAIN; PROTEIN FUNCTION; PROTEIN PHOSPHORYLATION; SARCOPLASMIC RETICULUM;

EID: 0037902618     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2003.tb07210.x     Document Type: Conference Paper

References (6)

1. LEE, A.G. & J.M. EAST. 2001. What the structure of a calcium pump tells us about its mechanism. Biochem. J. 356: 665-683.
2. TOYOSHIMA, C. et al. 2000. Crystal structure of the calcium pump of sarcoplasmic reticulum at 2.6 Å resolution. Nature 405: 647-655.
3. CORNELL, W.D. & S. LOUISE-MAY. 1998. Normal mode analysis. In Encyclopedia of Computational Chemistry, pp. 1904-1913. Wiley. Chichester/New York.
4. HINSEN, K. 1998. Analysis of domain motions by approximate normal mode calculations. Proteins 33: 417-429.
5. HINSEN, K. 2000. The Molecular Modeling Toolkit: a new approach to molecular simulations. J. Comput. Chem. 21: 79-85.
6. 2+-ATPase. J. Mol. Biol. 316: 201-211.