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.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1993
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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.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1996
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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.
Publication Name: Cell
Subject: Biological sciences
ISSN: 0092-8674
Year: 1997
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- Abstracts: Modular binding domains in signal transduction proteins. Specificity in signal transduction: from phosphotyrosine-SH2 domain interactions to complex cellular systems
- Abstracts: Binding affinities and cooperative interactions with bHLH activators delimit threshold responses to the dorsal gradient morphogen