View source for 2ceh


==Phosphorylation of the Cytoplasmic Tail of Tissue Factor and its Role in Modulating Structure and Binding Affinity==
<StructureSection load='2ceh' size='340' side='right'caption='[[2ceh]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[2ceh]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2CEH OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2CEH FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr>
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2ceh FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2ceh OCA], [https://pdbe.org/2ceh PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2ceh RCSB], [https://www.ebi.ac.uk/pdbsum/2ceh PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2ceh ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/TF_HUMAN 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.<ref>PMID:12652293</ref> 
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== 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<ref>PMID:20076769</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 2ceh" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Agrawal S]]
[[Category: Craft JW]]
[[Category: Legge GB]]
[[Category: Ruf W]]
[[Category: Sen M]]