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4D2G

Crystal structure of human PCNA in complex with p15 peptide

4D2G の概要
エントリーDOI10.2210/pdb4d2g/pdb
分子名称PROLIFERATING CELL NUCLEAR ANTIGEN, P15 (3 entities in total)
機能のキーワードtranscription
由来する生物種HOMO SAPIENS (HUMAN)
詳細
細胞内の位置Nucleus : P12004
タンパク質・核酸の鎖数5
化学式量合計91875.62
構造登録者
主引用文献De Biasio, A.,De Opakua, A.I.,Mortuza, G.B.,Molina, R.,Cordeiro, T.N.,Castillo, F.,Villate, M.,Merino, N.,Delgado, S.,Gil-Carton, D.,Luque, I.,Diercks, T.,Bernado, P.,Montoya, G.,Blanco, F.J.
Structure of P15(Paf)-PCNA Complex and Implications for Clamp Sliding During DNA Replication and Repair.
Nat.Commun., 6:6439-, 2015
Cited by
PubMed Abstract: The intrinsically disordered protein p15(PAF) regulates DNA replication and repair by binding to the proliferating cell nuclear antigen (PCNA) sliding clamp. We present the structure of the human p15(PAF)-PCNA complex. Crystallography and NMR show the central PCNA-interacting protein motif (PIP-box) of p15(PAF) tightly bound to the front-face of PCNA. In contrast to other PCNA-interacting proteins, p15(PAF) also contacts the inside of, and passes through, the PCNA ring. The disordered p15(PAF) termini emerge at opposite faces of the ring, but remain protected from 20S proteasomal degradation. Both free and PCNA-bound p15(PAF) binds DNA mainly through its histone-like N-terminal tail, while PCNA does not, and a model of the ternary complex with DNA inside the PCNA ring is consistent with electron micrographs. We propose that p15(PAF) acts as a flexible drag that regulates PCNA sliding along the DNA and facilitates the switch from replicative to translesion synthesis polymerase binding.
PubMed: 25762514
DOI: 10.1038/NCOMMS7439
主引用文献が同じPDBエントリー
実験手法
X-RAY DIFFRACTION (2.65 Å)
構造検証レポート
Validation report summary of 4d2g
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2026-02-04に公開中

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