1cvq
From Proteopedia
(New page: 200px<br /> <applet load="1cvq" size="450" color="white" frame="true" align="right" spinBox="true" caption="1cvq" /> '''SOLUTION STRUCTURE OF THE ANALOGUE RETRO-IN...) |
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'''SOLUTION STRUCTURE OF THE ANALOGUE RETRO-INVERSO MGREGRIGGC IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 7 STRUCTURES'''<br /> | '''SOLUTION STRUCTURE OF THE ANALOGUE RETRO-INVERSO MGREGRIGGC IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 7 STRUCTURES'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1CVQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with NH2 as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1CVQ is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/ ] with <scene name='pdbligand=NH2:'>NH2</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CVQ OCA]. |
==Reference== | ==Reference== | ||
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[[Category: tr-noe]] | [[Category: tr-noe]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:37:29 2008'' |
Revision as of 13:37, 15 February 2008
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SOLUTION STRUCTURE OF THE ANALOGUE RETRO-INVERSO MGREGRIGGC IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 7 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
1CVQ is a Protein complex structure of sequences from [1] with as ligand. 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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