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| | ==Solution structure of the human Raf-1 kinase inhibitor protein== | | ==Solution structure of the human Raf-1 kinase inhibitor protein== |
| - | <StructureSection load='2l7w' size='340' side='right' caption='[[2l7w]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''> | + | <StructureSection load='2l7w' size='340' side='right'caption='[[2l7w]]' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[2l7w]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2L7W OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2L7W FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[2l7w]] 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=2L7W OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2L7W FirstGlance]. <br> |
| - | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">RKIP ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr> | + | </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'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=2l7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l7w OCA], [http://pdbe.org/2l7w PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=2l7w RCSB], [http://www.ebi.ac.uk/pdbsum/2l7w PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=2l7w ProSAT]</span></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=2l7w FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2l7w OCA], [https://pdbe.org/2l7w PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2l7w RCSB], [https://www.ebi.ac.uk/pdbsum/2l7w PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2l7w ProSAT]</span></td></tr> |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PEBP1_HUMAN 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.<ref>PMID:18294816</ref> 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).<ref>PMID:18294816</ref> | + | [https://www.uniprot.org/uniprot/PEBP1_HUMAN 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.<ref>PMID:18294816</ref> 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).<ref>PMID:18294816</ref> |
| | == References == | | == References == |
| | <references/> | | <references/> |
| | __TOC__ | | __TOC__ |
| | </StructureSection> | | </StructureSection> |
| - | [[Category: Human]] | + | [[Category: Homo sapiens]] |
| - | [[Category: Yi, C Y]] | + | [[Category: Large Structures]] |
| - | [[Category: Raf-1 kinase inhibitor protein]] | + | [[Category: Yi CY]] |
| - | [[Category: Signaling protein inhibitor]]
| + | |
| Structural highlights
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]
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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