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| Reference: |
Blancuzzi Y, Padilla A, Parello J, Cave ASymmetrical rearrangement of the cation-binding sites of parvalbumin upon Ca2+/Mg2+ exchange. A study by 1H 2D NMRBiochemistry v32, p.1302-1309Two forms of parvalbumin, i.e., the fully Ca-loaded form PaCa2 and the fully Mg-loaded form PaMg2, are investigated by 2D 1H NMR in solution. A detailed analysis of the resonances, which belong to residues involved in direct coordination of Ca2+ and Mg2+, establishes that the sixth ligand, a highly conserved Glu residue at the relative position 12 in both cation-binding sites CD and EF, undergoes a conformational rearrangement through a 120 degrees rotation of its side chain about the C alpha-C beta bond with PaMg2 adopting the less energetically favored g- conformation, as inferred from scalar coupling constants and dipole-dipole contacts measured on the COSY and NOESY spectra, respectively....
All References |
| Description: |
Parvalbumin (Alpha Lineage, Pi 5.0) Complexed With Calcium (Nmr, Average Structure). |
| Deposition: |
1994/3/22  |
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| Author: |
Padilla A, Cave A, Parello J, Etienne G, Baldellon C |
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| Taxonomy: |
Esox lucius |
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Molecular components in the MMDB structure are listed below and may include macromolecular chains, 3D domains, protein classifications (domain families), and ligands, as available. Mouse over each icon for more information on the component. 
Citing MMDB:
Wang Y, Addess KJ, Chen J, Geer LY, He J, He S, Lu S, Madej T, Marchler-Bauer A, Thiessen PA, Zhang N, Bryant SH.
"MMDB: annotating protein sequences with Entrez's 3D-structure database.",
Nucleic Acids Res. 2007 Jan; 35(Database issue): D298-300.
Chen J, Anderson JB, DeWeese-Scott C, Fedorova ND, Geer LY, He S, Hurwitz DI, Jackson JD, Jacobs AR, Lanczycki CJ, Liebert CA, Liu C, Madej T, Marchler-Bauer A, Marchler GH, Mazumder R, Nikolskaya AN, Rao BS, Panchenko AR, Shoemaker BA, Simonyan V, Song JS, Thiessen PA, Vasudevan S, Wang Y, Yamashita RA, Yin JJ, Bryant SH.
"MMDB: Entrez's 3D-structure database", Nucleic Acids Res. 2003 Jan; 31(1): 474-7.
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