1kn3: Difference between revisions
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== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1kn3]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KN3 FirstGlance]. <br> | <table><tr><td colspan='2'>[[1kn3]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1KN3 FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bd9|1bd9]], [[1beh|1beh]], [[1a44|1a44]], [[1qou|1qou]], [[1fjj|1fjj]], [[1fux|1fux]]</td></tr> | </td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bd9|1bd9]], [[1beh|1beh]], [[1a44|1a44]], [[1qou|1qou]], [[1fjj|1fjj]], [[1fux|1fux]]</td></tr> | ||
<tr><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 Mus musculus])</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 Mus musculus])</td></tr> | ||
<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1kn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kn3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kn3 RCSB], [http://www.ebi.ac.uk/pdbsum/1kn3 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=1kn3 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1kn3 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1kn3 RCSB], [http://www.ebi.ac.uk/pdbsum/1kn3 PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Function == | |||
[[http://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: Mus musculus]] | [[Category: Mus musculus]] | ||
[[Category: Banfield, M J | [[Category: Banfield, M J]] | ||
[[Category: Brady, R L | [[Category: Brady, R L]] | ||
[[Category: Simister, P C | [[Category: Simister, P C]] | ||
[[Category: Cis-peptide]] | [[Category: Cis-peptide]] | ||
[[Category: Phosphatidylethanolamine binding]] | [[Category: Phosphatidylethanolamine binding]] | ||
[[Category: Protein binding]] | [[Category: Protein binding]] | ||
[[Category: Raf-1 kinase inhibitor]] | [[Category: Raf-1 kinase inhibitor]] | ||
Revision as of 01:43, 25 December 2014
Murine PEBP-2 (phosphatidylethanolamine-binding protein-2)Murine PEBP-2 (phosphatidylethanolamine-binding protein-2)
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 PubMedProteins 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 |
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