2cef

Phosphorylation of the Cytoplasmic Tail of Tissue Factor and its Role in Modulating Structure and Binding Affinity

spinqualitylabelsall models 2cef, 10 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2cef is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. NonStd Res: SEP Related: 1ahw, 1boy, 1dan, 1fak, 1j9c, 1jps, 1nl8, 1o5d, 1tfh, 1uj3, 1w0y, 1w2k, 1wqv, 1wss, 1wtg, 1wun, 1wv7, 1z6j, 2c4f, 2ceh, 2cez, 2cfj, 2hft Resources: FirstGlance, OCA, PDBe, RCSB, PDBsum Function [TF_HUMAN] Initiates blood coagulation by forming a complex with circulating factor VII or VIIa. The [TF:VIIa] complex activates factors IX or X by specific limited protolysis. TF plays a role in normal hemostasis by initiating the cell-surface assembly and propagation of the coagulation protease cascade. Publication Abstract from PubMed Tissue Factor (TF) is well known for its role during the activation of the coagulation pathway, but it is also critical for tumor biology and inflammation through protease activated receptor (PAR) 2 signaling. This signaling function is modulated by the successive phosphorylation of residues Ser253 and Ser258 within the TF cytoplasmic region (TFCR). This paper reports how we used NMR and spectroscopic methods to investigate the structural propensities of the unphosphorylated and phosphorylated forms of the TFCR. When unphosphorylated, the TFCR forms a local hydrophobic collapse around Trp254 and an electropositive patch from the membrane proximal basic block (Arg246-Lys247) to the conserved PKCalpha consensus residue Lys255. Phosphorylation of Ser253 alters the charge characteristics of this membrane proximal region, thereby strengthening the interaction between residue Ala248 and the Trp254 aromatic group. Phosphorylation of the Ser258-Pro259 motif destabilizes a turn at the C-terminus to form an extended polyproline helical motif. Our data suggests that by changing both its charge and local structural propensity, covalent modifications of the TFCR can potentially regulate its association with the cellular membrane and its signaling partners. Spectroscopic Characterization of Successive Phosphorylation of the Tissue Factor Cytoplasmic Region.,Sen M, Herzik M, Craft JW, Creath AL, Agrawal S, Ruf W, Legge GB Open Spectrosc J. 2009 Jan 1;3:58-64. PMID:20076769 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

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