1CZ2
SOLUTION STRUCTURE OF WHEAT NS-LTP COMPLEXED WITH PROSTAGLANDIN B2.
Summary for 1CZ2
| Entry DOI | 10.2210/pdb1cz2/pdb |
| Descriptor | NONSPECIFIC LIPID TRANSFER PROTEIN, PROSTAGLANDIN B2 (2 entities in total) |
| Functional Keywords | protein complex alpha helix, lipid binding protein |
| Biological source | Triticum aestivum (bread wheat) |
| Total number of polymer chains | 1 |
| Total formula weight | 9953.31 |
| Authors | Tassin-Moindrot, S.,Caille, A.,Douliez, J.-P.,Marion, D.,Vovelle, F. (deposition date: 1999-09-01, release date: 2000-09-27, Last modification date: 2024-11-20) |
| Primary citation | Tassin-Moindrot, S.,Caille, A.,Douliez, J.P.,Marion, D.,Vovelle, F. The wide binding properties of a wheat nonspecific lipid transfer protein. Solution structure of a complex with prostaglandin B2. Eur.J.Biochem., 267:1117-1124, 2000 Cited by PubMed Abstract: The 3D solution structure of wheat nonspecific lipid transfer protein (ns-LTP) complexed with prostaglandin B2, a lipid with both vinyl and hydroxylated groups, has been determined by 1H 2D NMR. The global fold of the protein is close to the previously published structures of wheat, maize, barley and rice ns-LTPs. The ligand is almost completely embedded in the hydrophobic core of the protein. Structure comparisons of free and bound wheat ns-LTP reveal that the binding of prostaglandin B2 hardly affects the global fold of the protein. The structural data on this unusual complex are discussed and compared with other known ns-LTP lipid-complexes. PubMed: 10672021DOI: 10.1046/j.1432-1327.2000.01109.x PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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