2qyq: Difference between revisions

Revision as of 10:38, 25 October 2017

Human raf kinase inhibitor protein (rkip) in complex with o-phosphotyrosineHuman raf kinase inhibitor protein (rkip) in complex with o-phosphotyrosine

Structural highlights

2qyq is a 1 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	1bd9, 1beh
Gene:	PEBP1, PBP, PEBP (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[PEBP1_HUMAN] Binds ATP, opioids and phosphatidylethanolamine. Has lower affinity for phosphatidylinositol and phosphatidylcholine. Serine protease inhibitor which inhibits thrombin, neuropsin and chymotrypsin but not trypsin, tissue type plasminogen activator and elastase (By similarity). Inhibits the kinase activity of RAF1 by inhibiting its activation and by dissociating the RAF1/MEK complex and acting as a competitive inhibitor of MEK phosphorylation.^[1] HCNP may be involved in the function of the presynaptic cholinergic neurons of the central nervous system. HCNP increases the production of choline acetyltransferase but not acetylcholinesterase. Seems to be mediated by a specific receptor (By similarity).^[2]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

References

↑ Rath O, Park S, Tang HH, Banfield MJ, Brady RL, Lee YC, Dignam JD, Sedivy JM, Kolch W, Yeung KC. The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK. Cell Signal. 2008 May;20(5):935-41. doi: 10.1016/j.cellsig.2008.01.012. Epub 2008, Jan 24. PMID:18294816 doi:http://dx.doi.org/10.1016/j.cellsig.2008.01.012
↑ Rath O, Park S, Tang HH, Banfield MJ, Brady RL, Lee YC, Dignam JD, Sedivy JM, Kolch W, Yeung KC. The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK. Cell Signal. 2008 May;20(5):935-41. doi: 10.1016/j.cellsig.2008.01.012. Epub 2008, Jan 24. PMID:18294816 doi:http://dx.doi.org/10.1016/j.cellsig.2008.01.012

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OCA

[1] Rath O, Park S, Tang HH, Banfield MJ, Brady RL, Lee YC, Dignam JD, Sedivy JM, Kolch W, Yeung KC. The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK. Cell Signal. 2008 May;20(5):935-41. doi: 10.1016/j.cellsig.2008.01.012. Epub 2008, Jan 24. PMID:18294816 doi:http://dx.doi.org/10.1016/j.cellsig.2008.01.012

[2] Rath O, Park S, Tang HH, Banfield MJ, Brady RL, Lee YC, Dignam JD, Sedivy JM, Kolch W, Yeung KC. The RKIP (Raf-1 Kinase Inhibitor Protein) conserved pocket binds to the phosphorylated N-region of Raf-1 and inhibits the Raf-1-mediated activated phosphorylation of MEK. Cell Signal. 2008 May;20(5):935-41. doi: 10.1016/j.cellsig.2008.01.012. Epub 2008, Jan 24. PMID:18294816 doi:http://dx.doi.org/10.1016/j.cellsig.2008.01.012

[1]

[2]

@@ Line 1: / Line 1: @@
 ==Human raf kinase inhibitor protein (rkip) in complex with o-phosphotyrosine==
 <StructureSection load='2qyq' size='340' side='right' caption='[[2qyq]], [[Resolution|resolution]] 1.95&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bd9|1bd9]], [[1beh|1beh]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">PEBP1, PBP, PEBP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=2qyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qyq OCA], [http://pdbe.org/2qyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qyq RCSB], [http://www.ebi.ac.uk/pdbsum/2qyq 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=2qyq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2qyq OCA], [http://pdbe.org/2qyq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2qyq RCSB], [http://www.ebi.ac.uk/pdbsum/2qyq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2qyq ProSAT]</span></td></tr>
 </table>
 == Function ==

2qyq: Difference between revisions

Revision as of 10:38, 25 October 2017

Human raf kinase inhibitor protein (rkip) in complex with o-phosphotyrosineHuman raf kinase inhibitor protein (rkip) in complex with o-phosphotyrosine

Structural highlights

Function

Evolutionary Conservation

References

Contents

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2qyq: Difference between revisions

Revision as of 10:38, 25 October 2017

Human raf kinase inhibitor protein (rkip) in complex with o-phosphotyrosineHuman raf kinase inhibitor protein (rkip) in complex with o-phosphotyrosine

Structural highlights

Function

Evolutionary Conservation

References

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