1sa8: Difference between revisions

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Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

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 ==THE NMR STRUCTURE OF A STABLE AND COMPACT ALL-beta-SHEET VARIANT OF INTESTINAL FATTY ACID-BINDING PROTEIN==
-<StructureSection load='1sa8' size='340' side='right'caption='[[1sa8]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''>
+<StructureSection load='1sa8' size='340' side='right'caption='[[1sa8]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1sa8]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SA8 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1SA8 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1sa8]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1SA8 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1SA8 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;'>[[1a57|1a57]], [[1ael|1ael]], [[1ure|1ure]]</div></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='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">FABP2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</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=1sa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sa8 OCA], [https://pdbe.org/1sa8 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1sa8 RCSB], [https://www.ebi.ac.uk/pdbsum/1sa8 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1sa8 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=1sa8 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1sa8 OCA], [http://pdbe.org/1sa8 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1sa8 RCSB], [http://www.ebi.ac.uk/pdbsum/1sa8 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1sa8 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/FABPI_RAT FABPI_RAT]] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor (By similarity).
+[https://www.uniprot.org/uniprot/FABPI_RAT FABPI_RAT] FABP are thought to play a role in the intracellular transport of long-chain fatty acids and their acyl-CoA esters. FABP2 is probably involved in triglyceride-rich lipoprotein synthesis. Binds saturated long-chain fatty acids with a high affinity, but binds with a lower affinity to unsaturated long-chain fatty acids. FABP2 may also help maintain energy homeostasis by functioning as a lipid sensor (By similarity).
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
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 __TOC__
 </StructureSection>
-[[Category: Buffalo rat]]
 [[Category: Large Structures]]
-[[Category: Cistola, D P]]
+[[Category: Rattus norvegicus]]
-[[Category: DeKoster, G T]]
+[[Category: Cistola DP]]
-[[Category: Ogbay, B]]
+[[Category: DeKoster GT]]
-[[Category: Intestinal fatty acid-binding protein]]
+[[Category: Ogbay B]]
-[[Category: Lipid binding protein]]
-[[Category: Protein stability]]
-[[Category: Protein structure]]