<p>The crystal structure of the SH2 domain of the Src-family kinase Lck bound to a high-affinity phosphotyrosyl peptide (PDB ID 1LCJ) [<a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0156218#pone.0156218.ref033" target="_blank">33</a>] is superimposed on the Jak2 SH2 domain. The Lck structure is shown as a white ribbon, with the bound phosphopeptide in green. The Jak2 SH2 domain is colored blue. The phosphotyrosine sidechain and selected residues in the binding pocket are shown in stick form. Note that Phe436 in the Jak2 SH2 domain blocks the position that would be occupied by the phenyl group of a bound phosphotyrosine. Labels refer to Jak2 residues.</p
ABSTRACT: The catalytic activity of Src-family kinases is regulated by association with its SH3 and ...
© 2012 Dr. Natalie Johanna GunnThe SH2 domain is an important regulatory module, and the involvement...
Src homology 2 (SH2) domains provide specificity to intracellular signaling by binding to specific p...
The crystal structure of the Src SH2 domain complexed with a high affinity 11-residue phosphopeptide...
The crystal structure of the Src SH2 domain complexed with a high affinity 11-residue phosphopeptide...
The binding properties of Src homology-2 (SH2) domains to phosphotyrosine (pY)-containing peptides h...
Src homology 2 (SH2) domains are found in a variety of signaling proteins and bind phosphotyrosine-c...
SummaryIn eukaryotic cells, the SH2 and PTB domains mediate protein-protein interactions by recogniz...
Src homology 2 (SH2) domains are modular protein struc-tures that bind phosphotyrosine (pY)-containi...
SH2 domain #1BFJ. Src-homology 2 (SH2) domains are modules of ~100 amino acids that bind to specific...
SH2 domains are phosphotyrosine specific interaction modules with largely overlapping sequence speci...
SH2 domains are phosphotyrosine specific interaction modules with largely overlapping sequence speci...
SH2 domain #1BFJ. Src-homology 2 (SH2) domains are modules of ~100 amino acids that bind to specific...
SH2 domains are phosphotyrosine specific interaction modules with largely overlapping sequence speci...
Nck proteins are essential Src homology SH 2 and SH3 domain bearing adapters that modulate actin c...
ABSTRACT: The catalytic activity of Src-family kinases is regulated by association with its SH3 and ...
© 2012 Dr. Natalie Johanna GunnThe SH2 domain is an important regulatory module, and the involvement...
Src homology 2 (SH2) domains provide specificity to intracellular signaling by binding to specific p...
The crystal structure of the Src SH2 domain complexed with a high affinity 11-residue phosphopeptide...
The crystal structure of the Src SH2 domain complexed with a high affinity 11-residue phosphopeptide...
The binding properties of Src homology-2 (SH2) domains to phosphotyrosine (pY)-containing peptides h...
Src homology 2 (SH2) domains are found in a variety of signaling proteins and bind phosphotyrosine-c...
SummaryIn eukaryotic cells, the SH2 and PTB domains mediate protein-protein interactions by recogniz...
Src homology 2 (SH2) domains are modular protein struc-tures that bind phosphotyrosine (pY)-containi...
SH2 domain #1BFJ. Src-homology 2 (SH2) domains are modules of ~100 amino acids that bind to specific...
SH2 domains are phosphotyrosine specific interaction modules with largely overlapping sequence speci...
SH2 domains are phosphotyrosine specific interaction modules with largely overlapping sequence speci...
SH2 domain #1BFJ. Src-homology 2 (SH2) domains are modules of ~100 amino acids that bind to specific...
SH2 domains are phosphotyrosine specific interaction modules with largely overlapping sequence speci...
Nck proteins are essential Src homology SH 2 and SH3 domain bearing adapters that modulate actin c...
ABSTRACT: The catalytic activity of Src-family kinases is regulated by association with its SH3 and ...
© 2012 Dr. Natalie Johanna GunnThe SH2 domain is an important regulatory module, and the involvement...
Src homology 2 (SH2) domains provide specificity to intracellular signaling by binding to specific p...