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| | <StructureSection load='1kn3' size='340' side='right'caption='[[1kn3]], [[Resolution|resolution]] 1.80Å' scene=''> | | <StructureSection load='1kn3' size='340' side='right'caption='[[1kn3]], [[Resolution|resolution]] 1.80Å' scene=''> |
| | == Structural highlights == | | == Structural highlights == |
| - | <table><tr><td colspan='2'>[[1kn3]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Lk3_transgenic_mice Lk3 transgenic mice]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KN3 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1KN3 FirstGlance]. <br> | + | <table><tr><td colspan='2'>[[1kn3]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1KN3 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1KN3 FirstGlance]. <br> |
| - | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bd9|1bd9]], [[1beh|1beh]], [[1a44|1a44]], [[1qou|1qou]], [[1fjj|1fjj]], [[1fux|1fux]]</div></td></tr> | + | </td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.8Å</td></tr> |
| - | <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">pebp-2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10090 LK3 transgenic mice])</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=1kn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kn3 OCA], [https://pdbe.org/1kn3 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1kn3 RCSB], [https://www.ebi.ac.uk/pdbsum/1kn3 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1kn3 ProSAT]</span></td></tr> |
| - | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1kn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kn3 OCA], [http://pdbe.org/1kn3 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1kn3 RCSB], [http://www.ebi.ac.uk/pdbsum/1kn3 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1kn3 ProSAT]</span></td></tr> | + | |
| | </table> | | </table> |
| | == Function == | | == Function == |
| - | [[http://www.uniprot.org/uniprot/PEBP2_MOUSE PEBP2_MOUSE]] May bind to phospholipids. May act as serine protease inhibitor (By similarity). | + | [https://www.uniprot.org/uniprot/PEBP2_MOUSE PEBP2_MOUSE] May bind to phospholipids. May act as serine protease inhibitor (By similarity). |
| | == Evolutionary Conservation == | | == Evolutionary Conservation == |
| | [[Image:Consurf_key_small.gif|200px|right]] | | [[Image:Consurf_key_small.gif|200px|right]] |
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| | </StructureSection> | | </StructureSection> |
| | [[Category: Large Structures]] | | [[Category: Large Structures]] |
| - | [[Category: Lk3 transgenic mice]] | + | [[Category: Mus musculus]] |
| - | [[Category: Banfield, M J]] | + | [[Category: Banfield MJ]] |
| - | [[Category: Brady, R L]] | + | [[Category: Brady RL]] |
| - | [[Category: Simister, P C]] | + | [[Category: Simister PC]] |
| - | [[Category: Cis-peptide]]
| + | |
| - | [[Category: Phosphatidylethanolamine binding]]
| + | |
| - | [[Category: Protein binding]]
| + | |
| - | [[Category: Raf-1 kinase inhibitor]]
| + | |
| Structural highlights
Function
PEBP2_MOUSE May bind to phospholipids. May act as serine protease inhibitor (By similarity).
Evolutionary Conservation
Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.
Publication Abstract from PubMed
Proteins from the PEBP (phosphatidylethanolamine-binding protein) family have been identified in a wide variety of species and are thought to regulate a range of intracellular signalling cascades. The rat homologue (known as RKIP; Raf-1 kinase inhibitor protein) has been shown to negatively regulate the MAP kinase pathway through formation of inhibitory complexes with Raf-1 and MEK. The crystal structure of a new, murine member of the PEBP family, termed mPEBP-2, has been determined. On the basis of amino-acid homology, mPEBP-2 belongs to a distinct subset of the mammalian PEBP proteins. Nonetheless, mPEBP-2 is seen to be very similar in structure to other PEBP proteins from human, bovine and plant sources. Regions of distinctive sequence associated with the PEBP-2 subset are discussed with reference to this structure.
The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family.,Simister PC, Banfield MJ, Brady RL Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1077-80. Epub, 2002 May 29. PMID:12037323[1]
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.
References
- ↑ Simister PC, Banfield MJ, Brady RL. The crystal structure of PEBP-2, a homologue of the PEBP/RKIP family. Acta Crystallogr D Biol Crystallogr. 2002 Jun;58(Pt 6 Pt 2):1077-80. Epub, 2002 May 29. PMID:12037323
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