2KTR
NMR structure of p62 PB1 dimer determined based on PCS
2KTR の概要
| エントリーDOI | 10.2210/pdb2ktr/pdb |
| 関連するPDBエントリー | 2KKC 2RPV |
| 分子名称 | Sequestosome-1, TERBIUM(III) ION (3 entities in total) |
| 機能のキーワード | autophagy, nf-kb signaling, homo-oligomer, pb1 dimer, signaling protein, transport protein |
| 由来する生物種 | Rattus norvegicus (Rat) 詳細 |
| 細胞内の位置 | Cytoplasm: O08623 O08623 |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 24391.13 |
| 構造登録者 | |
| 主引用文献 | Saio, T.,Yokochi, M.,Kumeta, H.,Inagaki, F. PCS-based structure determination of protein-protein complexes J.Biomol.Nmr, 46:271-280, 2010 Cited by PubMed Abstract: A simple and fast nuclear magnetic resonance method for docking proteins using pseudo-contact shift (PCS) and (1)H(N)/(15)N chemical shift perturbation is presented. PCS is induced by a paramagnetic lanthanide ion that is attached to a target protein using a lanthanide binding peptide tag anchored at two points. PCS provides long-range (approximately 40 A) distance and angular restraints between the lanthanide ion and the observed nuclei, while the (1)H(N)/(15)N chemical shift perturbation data provide loose contact-surface information. The usefulness of this method was demonstrated through the structure determination of the p62 PB1-PB1 complex, which forms a front-to-back 20 kDa homo-oligomer. As p62 PB1 does not intrinsically bind metal ions, the lanthanide binding peptide tag was attached to one subunit of the dimer at two anchoring points. Each monomer was treated as a rigid body and was docked based on the backbone PCS and backbone chemical shift perturbation data. Unlike NOE-based structural determination, this method only requires resonance assignments of the backbone (1)H(N)/(15)N signals and the PCS data obtained from several sets of two-dimensional (15)N-heteronuclear single quantum coherence spectra, thus facilitating rapid structure determination of the protein-protein complex. PubMed: 20300805DOI: 10.1007/s10858-010-9401-4 主引用文献が同じPDBエントリー |
| 実験手法 | SOLUTION NMR |
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