1ct6: Difference between revisions
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==SOLUTION STRUCTURE OF CGGIRGERG IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 11 STRUCTURES== | ==SOLUTION STRUCTURE OF CGGIRGERG IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 11 STRUCTURES== | ||
<StructureSection load='1ct6' size='340' side='right'caption='[[1ct6 | <StructureSection load='1ct6' size='340' side='right'caption='[[1ct6]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ct6]] is a 1 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CT6 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1ct6]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CT6 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1CT6 FirstGlance]. <br> | ||
</td></tr><tr id=' | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | ||
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ct6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ct6 OCA], [https://pdbe.org/1ct6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ct6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ct6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ct6 ProSAT]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ct6 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ct6 OCA], [https://pdbe.org/1ct6 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ct6 RCSB], [https://www.ebi.ac.uk/pdbsum/1ct6 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ct6 ProSAT]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[https://www.uniprot.org/uniprot/H31_HUMAN H31_HUMAN] | |||
<div style="background-color:#fffaf0;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: Homo sapiens]] | |||
[[Category: Large Structures]] | [[Category: Large Structures]] | ||
[[Category: Briand | [[Category: Briand JP]] | ||
[[Category: Cung | [[Category: Cung MT]] | ||
[[Category: Guichard G]] | |||
[[Category: Guichard | [[Category: Muller S]] | ||
[[Category: Muller | [[Category: Petit MC]] | ||
[[Category: Petit | [[Category: Phan Chan Du A]] | ||
[[Category: | |||
Latest revision as of 14:41, 22 November 2023
SOLUTION STRUCTURE OF CGGIRGERG IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 11 STRUCTURESSOLUTION STRUCTURE OF CGGIRGERG IN CONTACT WITH THE MONOCLONAL ANTIBODY MAB 4X11, NMR, 11 STRUCTURES
Structural highlights
FunctionPublication Abstract from PubMedThe 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. 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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