4LVE
LEN K30T MUTANT: A DOMAIN FLIP AS A RESULT OF A SINGLE AMINO ACID SUBSTITUTION
4LVE の概要
| エントリーDOI | 10.2210/pdb4lve/pdb |
| 分子名称 | LEN (2 entities in total) |
| 機能のキーワード | immunoglobulin, kappa-iv, light chain dimer |
| 由来する生物種 | Homo sapiens (human) |
| タンパク質・核酸の鎖数 | 2 |
| 化学式量合計 | 25243.87 |
| 構造登録者 | |
| 主引用文献 | Pokkuluri, P.R.,Huang, D.B.,Raffen, R.,Cai, X.,Johnson, G.,Stevens, P.W.,Stevens, F.J.,Schiffer, M. A domain flip as a result of a single amino-acid substitution. Structure, 6:1067-1073, 1998 Cited by PubMed Abstract: The self-assembly properties of beta domains are important features of diverse classes of proteins that include cell-adhesion molecules, surface receptors and the immunoglobulin superfamily. Immunoglobulin light-chain variable domains are well suited to the study of structural factors that determine dimerization, including how residues at the interface influence the preferred dimer arrangement. PubMed: 9739086DOI: 10.1016/S0969-2126(98)00107-5 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (2.3 Å) |
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