FES + staurosporin

FES + staurosporin

FES + staurosporin: Human feline sarcoma oncogene + staurosporin
PDB Code: 3BKB
Fes forms with Fer a separate family of the non-receptor protein tyrosine kinase. Both proteins share a similar domain organization comprising a unique N-terminal Fps/Fes/Fer/CIP4 homology (FCH) domain, regions of predicted coiled coils (CC), a central Src homology 2 (SH2) domain, and a C-terminal tyrosine kinase domain. The coiled-coil motif in Fps/Fes is thought to have an auto-regulatory function and a model has been proposed in which the coiled-coil domains regulate interconversion between inactive monomers and (auto)-activated oligomers.
Fes is involved in several processes in the function of hematopioetic cells including regulation of innate immune response, hematopoiesis, regulation of angiogenesis and it may play a general role in the regulation of vesicular trafficking and microtubule dynamics including microtubule nucleation and bundling. In addition, Fes is a regulator of inflammation and plays a role in leucocyte recruitment to areas of inflammation.
Interestingly, a proto-oncogene as well as a tumor suppressor function has been proposed. For instance, in acute promyelocytic leukemia the chromosomal location of Fes has been linked to a specific translocation event and activation of Fes can mediate cellular transformation. In addition, elevated expression levels of Fes are found in adult human myeloid leukemia cells and transgenic mice, expression of Gag–Fps/Fes under the control of a heterologous promoter, develop tumors in lymphoid and mesencymal tissues.
On the other hand, reduced expression of Fes has been described in anaplastic thyroid cancers and colorectal cancers. Introduction of Fes into these lines with a recombinant retrovirus suppresses cell growth in soft agar and missense mutations in sequences encoding the kinase domain of Fes have been described in a screen of human colorectal cancer that lead to Fes inactivation.
In contrast to Src, Hck and Abl, Fes/Fer does not posses an SH3 domain and can therefore not assume an auto-inhibited state in which the SH2/SH3 unit suppresses kinase activity. In order to shed light on the regulation of FES we determined the structure of the SH2-kinase domain at high resolution of the apo-protein (3BKB), mono-phosphorylated FES (3CD3) as well as inactive FES (3CBL) in complex with a consensus kinase substrate peptide.

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