6WBJ
High resolution crystal structure of mRECK(CC4) in fusion with engineered MBP
6WBJ の概要
| エントリーDOI | 10.2210/pdb6wbj/pdb |
| 関連するPDBエントリー | 6WBH |
| 関連するBIRD辞書のPRD_ID | PRD_900001 |
| 分子名称 | Maltodextrin-binding protein,Reversion-inducing cysteine-rich protein with Kazal motifs fusion, alpha-D-glucopyranose-(1-4)-alpha-D-glucopyranose, SULFATE ION, ... (6 entities in total) |
| 機能のキーワード | wnt signaling, 4-helix bundle, extracellular domain, vascularization, blood-brain barrier, maltose-binding protein, signaling protein |
| 由来する生物種 | Escherichia coli 詳細 |
| タンパク質・核酸の鎖数 | 1 |
| 化学式量合計 | 49757.74 |
| 構造登録者 | Chang, T.H.,Hsieh, F.L.,Gabelli, S.B.,Nathans, J. (登録日: 2020-03-26, 公開日: 2020-06-17, 最終更新日: 2024-10-23) |
| 主引用文献 | Chang, T.H.,Hsieh, F.L.,Smallwood, P.M.,Gabelli, S.B.,Nathans, J. Structure of the RECK CC domain, an evolutionary anomaly. Proc.Natl.Acad.Sci.USA, 117:15104-15111, 2020 Cited by PubMed Abstract: Five small protein domains, the CC-domains, at the N terminus of the RECK protein, play essential roles in signaling by WNT7A and WNT7B in the context of central nervous system angiogenesis and blood-brain barrier formation and maintenance. We have determined the structure of CC domain 4 (CC4) at 1.65-Å resolution and find that it folds into a compact four-helix bundle with three disulfide bonds. The CC4 structure, together with homology modeling of CC1, reveals the surface locations of critical residues that were shown in previous mutagenesis studies to mediate GPR124 binding and WNT7A/WNT7B recognition and signaling. Surprisingly, sequence and structural homology searches reveal no other cell-surface or secreted domains in vertebrates that resemble the CC domain, a pattern that is in striking contrast to other ancient and similarly sized domains, such as Epidermal Growth Factor, Fibronectin Type 3, Immunoglobulin, and Thrombospondin type 1 domains, which are collectively present in hundreds of proteins. PubMed: 32541044DOI: 10.1073/pnas.2006332117 主引用文献が同じPDBエントリー |
| 実験手法 | X-RAY DIFFRACTION (1.651 Å) |
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