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1LPL

Structural Genomics of Caenorhabditis elegans: CAP-Gly domain of F53F4.3

1LPL の概要
エントリーDOI10.2210/pdb1lpl/pdb
分子名称Hypothetical 25.4 kDa protein F53F4.3 in chromosome V (2 entities in total)
機能のキーワードstructural genomics, cap-gly domain, cytoskeleton, tubulin, psi, protein structure initiative, southeast collaboratory for structural genomics, secsg, unknown function
由来する生物種Caenorhabditis elegans
細胞内の位置Cytoplasm (By similarity): Q20728
タンパク質・核酸の鎖数1
化学式量合計10358.67
構造登録者
主引用文献Li, S.,Finley, J.,Liu, Z.-J.,Qiu, S.H.,Luan, C.H.,Carson, M.,Tsao, J.,Johnson, D.,Lin, G.,Zhao, J.,Thomas, W.,Nagy, L.A.,Sha, B.,DeLucas, L.J.,Wang, B.-C.,Luo, M.
Crystal Structure of the Cytoskeleton-associated Protein Glycine-rich (CAP-Gly) Domain
J.Biol.Chem., 277:48596-48601, 2002
Cited by
PubMed Abstract: Cytoskeleton-associated proteins (CAPs) are involved in the organization of microtubules and transportation of vesicles and organelles along the cytoskeletal network. A conserved motif, CAP-Gly, has been identified in a number of CAPs, including CLIP-170 and dynactins. The crystal structure of the CAP-Gly domain of Caenorhabditis elegans F53F4.3 protein, solved by single wavelength sulfur-anomalous phasing, revealed a novel protein fold containing three beta-sheets. The most conserved sequence, GKNDG, is located in two consecutive sharp turns on the surface, forming the entrance to a groove. Residues in the groove are highly conserved as measured from the information content of the aligned sequences. The C-terminal tail of another molecule in the crystal is bound in this groove.
PubMed: 12221106
DOI: 10.1074/jbc.M208512200
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (1.77 Å)
構造検証レポート
Validation report summary of 1lpl
検証レポート(詳細版)ダウンロードをダウンロード

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件を2025-12-31に公開中

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