1F6L
VARIABLE LIGHT CHAIN DIMER OF ANTI-FERRITIN ANTIBODY
1F6L の概要
| エントリーDOI | 10.2210/pdb1f6l/pdb |
| 分子名称 | ANTI-FERRITIN IMMUNOGLOBULIN LIGHT CHAIN (2 entities in total) |
| 機能のキーワード | immunoglobulin fold, variable light chain, dimer, anti-ferritin antibody, immune system |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 12709.07 |
| 構造登録者 | Nymalm, Y.,Kravchuk, Z.,Salminen, T.,Chumanevich, A.A.,Dubnovitsky, A.P.,Kankare, J.,Pentikainen, O.,Lehtonen, J.,Arosio, P.,Martsev, S.,Johnson, M.S. (登録日: 2000-06-22, 公開日: 2002-10-23, 最終更新日: 2024-11-20) |
| 主引用文献 | Nymalm, Y.,Kravchuk, Z.,Salminen, T.,Chumanevich, A.A.,Dubnovitsky, A.P.,Kankare, J.,Pentikainen, O.,Lehtonen, J.,Arosio, P.,Martsev, S.,Johnson, M.S. Antiferritin VL homodimer binds human spleen ferritin with high specificity J.STRUCT.BIOL., 138:171-186, 2002 Cited by PubMed Abstract: The antiferritin variable light domain (VL) dimer binds human spleen ferritin ( approximately 85% L subunits) but with approximately 50-fold lower affinity, K(a)=4 x 10(7) x M(-1), than the parent F11 antibody (K(a)=2.1 x 10(9) x M(-1)). The VL dimer does not recognize either rL (100% L subunits) or rH (100% H subunits) human ferritin, whereas the parent antibody recognizes rL-ferritin. To help explain the differences in ferritin binding affinities and specificities, the crystal structure of the VL domain (2.8A resolution) was determined by molecular replacement and models of the antiferritin VL-VH dimer were made on the basis of antilysozyme antibody D1.3. The domain interface is smaller in the VL dimer but a larger number of interdomain hydrogen bonds may prevent rearrangement on antigen binding. The antigen binding surface of the VL dimer is flatter, lacking a negatively charged pocket found in the VL-VH models, contributed by the CDR3 loop of the VH domain. Loop CDR2 (VL dimer) is located away from the antigen binding site, while the corresponding loop of the VH domain would be located within the antigen binding site. Together these differences lead to 50-fold lower binding affinity in the VL dimer and to more restricted specificity than is seen for the parent antibody. PubMed: 12217656DOI: 10.1016/S1047-8477(02)00015-1 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.8 Å) |
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