Hapten conformation in the combining site of antibodies that bind phenylphosphocholine

We have shown previously that anti-phenylphosphocholine antibodies elicited by phosphocholine-keyhole limpet hemocyanin can be divided into two populations according to their ability to recognize the two hapten analogues p-nitrophenylphosphocholine (NPPC) and p-nitrophenyl 3,3-dimethylbutyl phosphat...

Celý popis

Uložené v:
Podrobná bibliografia
Vydané v:Biochemistry (Easton) Ročník 31; číslo 2; s. 584
Hlavní autori: Bruderer, U, Peyton, D H, Barbar, E, Fellman, J H, Rittenberg, M B
Médium: Journal Article
Jazyk:English
Vydavateľské údaje: United States 01.01.1992
Predmet:
Antibodies, Monoclonal - chemistry
Binding Sites, Antibody
Haptens - chemistry
Haptens - immunology
Magnetic Resonance Spectroscopy
Nitrophenols - chemistry
Nitrophenols - immunology
Phosphorylcholine - analogs & derivatives
Phosphorylcholine - chemistry
Phosphorylcholine - immunology
Protein Conformation
Spectrophotometry, Infrared
ISSN:0006-2960
On-line prístup:Zistit podrobnosti o prístupe
Tagy: Pridať tag
Žiadne tagy, Buďte prvý, kto otaguje tento záznam!
Popis
Shrnutí:We have shown previously that anti-phenylphosphocholine antibodies elicited by phosphocholine-keyhole limpet hemocyanin can be divided into two populations according to their ability to recognize the two hapten analogues p-nitrophenylphosphocholine (NPPC) and p-nitrophenyl 3,3-dimethylbutyl phosphate (NPDBP). These analogues differ from each other in that NPPC has a positively charged nitrogen in the choline moiety, whereas NPDBP lacks the positively charged nitrogen. Group II-A antibodies bind only NPPC, whereas group II-B antibodies bind both ligands. Here, by infrared and nuclear magnetic resonance spectroscopic investigations, we find that when free in solution NPPC has a predominantly fixed structure in which the termini approach each other, probably due to electrostatic interactions within the molecule; this "bent" structural feature is retained when the ligand is bound by antibody. In contrast, the structure of unbound NPDBP is less fixed, being characterized by rapidly interchanging conformations corresponding to an open chain structure with less overall proximity of the termini compared to NPPC. The overall shape of NPPC is essentially unaltered by binding, whereas in the case of NPDBP what was a minor conformation in the unbound state becomes the predominate conformation of the bound ligand. Thus, our results are consistent with these antibodies providing a molecular template for stabilizing the conformation of the bound ligand.
Bibliografia:ObjectType-Article-1
SourceType-Scholarly Journals-1
ObjectType-Feature-2
content type line 23
ISSN:0006-2960
DOI:10.1021/bi00117a040