4EIK

Crystal Structure of the Human Fyn SH3 domain in complex with the synthetic peptide VSL12

4EIK の概要

• エントリーDOI: 10.2210/pdb4eik/pdb
• 関連するPDBエントリー: 3UA6 3UA7
• 分子名称: Tyrosine-protein kinase Fyn, VSL12 peptide, SODIUM ION, ... (4 entities in total)
• 機能のキーワード: beta barrel, proline rich motifs, transferase-protein binding complex, transferase/protein binding
• 由来する生物種: Homo sapiens; 詳細
• 細胞内の位置: Cytoplasm: P06241
• タンパク質・核酸の鎖数: 2
• 化学式量合計: 8512.38

構造登録者

Camara-Artigas, A. (登録日: 2012-04-05, 公開日: 2013-04-10, 最終更新日: 2023-09-13)

主引用文献

Chen, Q.,Georgiadis, M.
Crystallization of and selenomethionine phasing strategy for a SETMAR-DNA complex.
Acta Crystallogr F Struct Biol Commun, 72:713-719, 2016

PubMed Abstract: Transposable elements have played a critical role in the creation of new genes in all higher eukaryotes, including humans. Although the chimeric fusion protein SETMAR is no longer active as a transposase, it contains both the DNA-binding domain (DBD) and catalytic domain of the Hsmar1 transposase. The amino-acid sequence of the DBD has been virtually unchanged in 50 million years and, as a consequence, SETMAR retains its sequence-specific binding to the ancestral Hsmar1 terminal inverted repeat (TIR) sequence. Thus, the DNA-binding activity of SETMAR is likely to have an important biological function. To determine the structural basis for the recognition of TIR DNA by SETMAR, the design of TIR-containing oligonucleotides and SETMAR DBD variants, crystallization of DBD-DNA complexes, phasing strategies and initial phasing experiments are reported here. An unexpected finding was that oligonucleotides containing two BrdUs in place of thymidines produced better quality crystals in complex with SETMAR than their natural counterparts.

PubMed: 27599863
DOI: 10.1107/S2053230X16012723

実験手法

X-RAY DIFFRACTION (1.6 Å)