1ct6
From Proteopedia
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==Overview== | ==Overview== | ||
| - | 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 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. |
==About this Structure== | ==About this Structure== | ||
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Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach., Phan-Chan-Du A, Petit MC, Guichard G, Briand JP, Muller S, Cung MT, Biochemistry. 2001 May 15;40(19):5720-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11341837 11341837] | Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach., Phan-Chan-Du A, Petit MC, Guichard G, Briand JP, Muller S, Cung MT, Biochemistry. 2001 May 15;40(19):5720-7. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11341837 11341837] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Briand, J | + | [[Category: Briand, J P.]] |
| - | [[Category: Cung, M | + | [[Category: Cung, M T.]] |
| - | [[Category: Du, A | + | [[Category: Du, A Phan Chan.]] |
[[Category: Guichard, G.]] | [[Category: Guichard, G.]] | ||
[[Category: Muller, S.]] | [[Category: Muller, S.]] | ||
| - | [[Category: Petit, M | + | [[Category: Petit, M C.]] |
[[Category: analogue]] | [[Category: analogue]] | ||
[[Category: antigen-antibody complex]] | [[Category: antigen-antibody complex]] | ||
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[[Category: tr-noe]] | [[Category: tr-noe]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 12:09:36 2008'' |
Revision as of 10:09, 21 February 2008
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SOLUTION STRUCTURE OF CGGIRGERG IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 11 STRUCTURES
Overview
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.
About this Structure
1CT6 is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.
Reference
Structure of antibody-bound peptides and retro-inverso analogues. A transferred nuclear Overhauser effect spectroscopy and molecular dynamics approach., Phan-Chan-Du A, Petit MC, Guichard G, Briand JP, Muller S, Cung MT, Biochemistry. 2001 May 15;40(19):5720-7. PMID:11341837
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