Binding of a high-affinity phosphotyrosyl peptide to the Src SH2 domain: crystal structures of the complexed and peptide-free forms

Article Abstract:

The crystal structure of the Src homology 2 (SH2) domains via X-ray diffraction is reported. SH2 is an important component of tyrosine phosphorylation-mediated cellular signal transduction. The SH2 crystal structure was analyzed in its free state at 2.5 Angstrom resolution and when bound to a high-affinity, 11-residue phosphotyrosyl peptide at 2.7 Angstrom resolution. Comparison of the high-affinity complex and the free SH2 revealed only localized and small differences in crystal structures.

Analysis, Peptides, Cellular signal transduction

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Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain

Article Abstract:

The nef gene's structure in complex with the SH3 domain of a mutant Fyn tyrosine kinase (where Arg-96 was substituted with isoleucine), was studied using X-ray crystallography. Analysis of the crystal structure showed the high affinity binding between Nef-SH3. Binding was effected by the PxxP motif in the folded structure of Nef, whose polyproline type II helix attaches to the SH3 domain. The PxxP sequence has been proven as an important component in viral replication.

Usage, HIV (Viruses), HIV, Viruses, X-ray crystallography

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Major domain swiveling revealed by the crystal structures of complexes of E. coli Rep helicase bound to single-stranded DNA and ADP

Article Abstract:

A study was conducted on the binary and ternary complexes' crystal structures in Escherichia coli Rep helicase bound to adenosine diphosphate and single-stranded DNA. Two Rep monomers with different reorientations were observed in the crystals' asymmetric unit. The helicase motifs for the adenosine diphosphate were found to be I and IV and those for the single-stranded DNA binding site were Ia, III and V.

Escherichia coli, Circular DNA, Adenosine diphosphate

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