4EIK

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

Summary for 4EIK

• Entry DOI: 10.2210/pdb4eik/pdb
• Related: 3UA6 3UA7
• Descriptor: Tyrosine-protein kinase Fyn, VSL12 peptide, SODIUM ION, ... (4 entities in total)
• Functional Keywords: beta barrel, proline rich motifs, transferase-protein binding complex, transferase/protein binding
• Biological source: Homo sapiens; More
• Cellular location: Cytoplasm: P06241
• Total number of polymer chains: 2
• Total formula weight: 8512.38

Authors

Camara-Artigas, A. (deposition date: 2012-04-05, release date: 2013-04-10, Last modification date: 2023-09-13)

Primary citation

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 Although the chimeric fusion protein SETMAR is no longer active as a transposase, it contains both the DNA-binding domain (DBD) and catalytic domain of the Hsmar1 transposase.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

Experimental method

X-RAY DIFFRACTION (1.6 Å)