2K2F
Solution structure of Ca2+-S100A1-RyRP12
Summary for 2K2F
| Entry DOI | 10.2210/pdb2k2f/pdb |
| NMR Information | BMRB: 15704 |
| Descriptor | Ryanodine receptor 1 peptide, Protein S100-A1, CALCIUM ION (3 entities in total) |
| Functional Keywords | s100, ef hand, ryanodine receptor, calcium binding, alternative splicing, calcium channel, calcium transport, glycoprotein, ion transport, ionic channel, membrane, polymorphism, transmembrane, transport, cytoplasm, metal-binding, zinc, metal binding protein |
| Biological source | Rattus norvegicus (rat) More |
| Cellular location | Cytoplasm: 2K2F |
| Total number of polymer chains | 4 |
| Total formula weight | 23981.18 |
| Authors | Wright, N.T.,Varney, K.M.,Weber, D.J. (deposition date: 2008-04-01, release date: 2008-07-29, Last modification date: 2024-05-29) |
| Primary citation | Wright, N.T.,Prosser, B.L.,Varney, K.M.,Zimmer, D.B.,Schneider, M.F.,Weber, D.J. S100A1 and Calmodulin Compete for the Same Binding Site on Ryanodine Receptor. J.Biol.Chem., 283:26676-26683, 2008 Cited by PubMed Abstract: In heart and skeletal muscle an S100 protein family member, S100A1, binds to the ryanodine receptor (RyR) and promotes Ca(2+) release. Using competition binding assays, we further characterized this system in skeletal muscle and showed that Ca(2+)-S100A1 competes with Ca(2+)-calmodulin (CaM) for the same binding site on RyR1. In addition, the NMR structure was determined for Ca(2+)-S100A1 bound to a peptide derived from this CaM/S100A1 binding domain, a region conserved in RyR1 and RyR2 and termed RyRP12 (residues 3616-3627 in human RyR1). Examination of the S100A1-RyRP12 complex revealed residues of the helical RyRP12 peptide (Lys-3616, Trp-3620, Lys-3622, Leu-3623, Leu-3624, and Lys-3626) that are involved in favorable hydrophobic and electrostatic interactions with Ca(2+)-S100A1. These same residues were shown previously to be important for RyR1 binding to Ca(2+)-CaM. A model for regulating muscle contraction is presented in which Ca(2+)-S100A1 and Ca(2+)-CaM compete directly for the same binding site on the ryanodine receptor. PubMed: 18650434DOI: 10.1074/jbc.M804432200 PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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