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2cez

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Revision as of 07:21, 17 January 2018

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

Structural highlights

2cez is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
NonStd Res:
Related:	1ahw, 1boy, 1dan, 1fak, 1j9c, 1jps, 1nl8, 1o5d, 1tfh, 1uj3, 1w0y, 1w2k, 1wqv, 1wss, 1wtg, 1wun, 1wv7, 1z6j, 2c4f, 2cef, 2ceh, 2hft, 2cfj
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

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.^[1]

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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Bogdanov VY, Balasubramanian V, Hathcock J, Vele O, Lieb M, Nemerson Y. Alternatively spliced human tissue factor: a circulating, soluble, thrombogenic protein. Nat Med. 2003 Apr;9(4):458-62. Epub 2003 Mar 24. PMID:12652293 doi:10.1038/nm841
↑ Sen M, Herzik M, Craft JW, Creath AL, Agrawal S, Ruf W, Legge GB. Spectroscopic Characterization of Successive Phosphorylation of the Tissue Factor Cytoplasmic Region. Open Spectrosc J. 2009 Jan 1;3:58-64. PMID:20076769 doi:http://dx.doi.org/10.2174/1874383800903010058

1 Structural highlights
2 Function
3 Publication Abstract from PubMed
4 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2cez"

@@ Line 1: / Line 1: @@
 ==Phosphorylation of the Cytoplasmic Tail of Tissue Factor and its Role in Modulating Structure and Binding Affinity==
 <StructureSection load='2cez' size='340' side='right' caption='[[2cez]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
@@ Line 5: / Line 6: @@
 </td></tr><tr id='NonStdRes'><td class="sblockLbl"><b>[[Non-Standard_Residue|NonStd Res:]]</b></td><td class="sblockDat"><scene name='pdbligand=SEP:PHOSPHOSERINE'>SEP</scene></td></tr>
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ahw|1ahw]], [[1boy|1boy]], [[1dan|1dan]], [[1fak|1fak]], [[1j9c|1j9c]], [[1jps|1jps]], [[1nl8|1nl8]], [[1o5d|1o5d]], [[1tfh|1tfh]], [[1uj3|1uj3]], [[1w0y|1w0y]], [[1w2k|1w2k]], [[1wqv|1wqv]], [[1wss|1wss]], [[1wtg|1wtg]], [[1wun|1wun]], [[1wv7|1wv7]], [[1z6j|1z6j]], [[2c4f|2c4f]], [[2cef|2cef]], [[2ceh|2ceh]], [[2hft|2hft]], [[2cfj|2cfj]]</td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cez OCA], [http://pdbe.org/2cez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cez RCSB], [http://www.ebi.ac.uk/pdbsum/2cez PDBsum]</span></td></tr>
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2cez FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2cez OCA], [http://pdbe.org/2cez PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2cez RCSB], [http://www.ebi.ac.uk/pdbsum/2cez PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2cez ProSAT]</span></td></tr>
 </table>
 == Function ==

2cez

From Proteopedia

Revision as of 07:21, 17 January 2018

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

Structural highlights

Function

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

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