A structural model of the complex formed by phospholamban and the calcium pump of sarcoplasmic reticulum obtained by molecular mechanics

ChemBioChem

Volumn 3, Issue 12, 2002, Pages 1200-1208

  Hutter, Michael C ^a   Krebs, Joachim ^b   Meiler, Jens ^c   Griesinger, Christian ^c   Carafoli, Ernesto ^d   Helms, Volkhard ^a  

^a MAX PLANCK INSTITUTE OF BIOPHYSICS   (Germany)

^b ETH ZURICH   (Switzerland)

^c GOETHE UNIVERSITY   (Germany)

^d VENETIAN INSTITUTE OF MOLECULAR MEDICINE   (Italy)

Author keywords

Enzyme models; Molecular modeling; Noncovalent interactions; Protein kinases; Protein structures

Indexed keywords

ADENOSINE TRIPHOSPHATASE (CALCIUM); CYCLIC AMP DEPENDENT PROTEIN KINASE; PHOSPHOLAMBAN;

AMINO TERMINAL SEQUENCE; ARTICLE; CALCIUM TRANSPORT; CRYSTAL STRUCTURE; MOLECULAR MODEL; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; SARCOPLASMIC RETICULUM;

ANIMALS; CALCIUM-BINDING PROTEINS; CALCIUM-TRANSPORTING ATPASES; HUMANS; HYDROGEN BONDING; MODELS, MOLECULAR; PROTEIN BINDING; SARCOPLASMIC RETICULUM;

EID: 12244255136     PISSN: 14394227     EISSN: None     Source Type: Journal    
DOI: 10.1002/1439-7633(20021202)3:12<1200::AID-CBIC1200>3.0.CO;2-H     Document Type: Article

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44. Note added in proof: After submitting this paper Toyoshima and Nomura published the crystal structure of an E2 form of the SERCA pump (Nature 2002, 418, 605) which was stabilized by the specific inhibitor thapsigargin (PDB code IWO). PLN does not seem to interact with the SERCA pump appropriately in the presence of thapsigargin (see Ref. [28]), but we have nevertheless modeled PLN into this new structure using M6 as the template. We applied the same procedure and the same constraints we had used for our optimal structure (Figure 1 of the paper). The results were less satisfactory, as can be seen by comparing Figure 6 provided in the Supporting information with Figure 1 b of the paper.