1CWZ
Solution structure of the analogue retro-inverso (MA-S)REGRIGGC in contact with the monoclonal antibody MAB 4X11, NMR, 7 structures
Summary for 1CWZ
| Entry DOI | 10.2210/pdb1cwz/pdb |
| Related | 1CS9 1CT6 1CVQ 1CW8 |
| Descriptor | HISTONE H3, METHYLMALONIC ACID (2 entities in total) |
| Functional Keywords | pseudomimetic, synthetic peptide, retro-inverso analogue, tr-noe, antigen- antibody complex, dna binding protein |
| Total number of polymer chains | 1 |
| Total formula weight | 965.07 |
| Authors | Phan Chan Du, A.,Petit, M.C.,Guichard, G.,Briand, J.P.,Muller, S.,Cung, M.T. (deposition date: 1999-08-27, release date: 1999-09-03, Last modification date: 2024-10-09) |
| Primary citation | Phan-Chan-Du, A.,Petit, M.C.,Guichard, G.,Briand, J.P.,Muller, S.,Cung, M.T. Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach. Biochemistry, 40:5720-5727, 2001 Cited by PubMed Abstract: The three-dimensional structures of the two L-peptides, H-CGGIRGERA-OH, called L(A), and H-CGGIRGERG-OH, called L(G), corresponding or close to the IRGERA sequence present in the C-terminal region (residues 130-135) of histone H3, and their retro-inverso analogues HO-mAreGriGGC-NH2, called RI(mA), and HO-mGreGriGGC-NH2, called RI(mG), have been studied by two-dimensional 1H NMR and molecular dynamics calculations in association with a monoclonal antibody generated against L(A). At 25 degrees C, the affinity constants of the monoclonal antibody with respect to RI(mA) and RI(mG) were 75- and 270-fold higher than those measured with the homologous L(A) and L(G) peptides, respectively. Due to the spontaneous epimerization of the mA malonic residue, RI(mA) gave rise to two sets of resonances. With regard to the NH amide region, one set was similar to that for RI(mG) while the second was similar to those for the parent L-peptides L(A) and L(G). The antibody-bound conformations of the two couples of L- and retro-inverso peptides have been analyzed using molecular modeling calculations based on the transferred NOE interproton distances. Folded structures appeared in both cases with a type II' beta-turn in the parent GGIR sequence and a type I' beta-turn in the retro-inverso reGr sequence. PubMed: 11341837DOI: 10.1021/bi001151h PDB entries with the same primary citation |
| Experimental method | SOLUTION NMR |
Structure validation
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