1cj5: Difference between revisions
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<StructureSection load='1cj5' size='340' side='right' caption='[[1cj5]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | <StructureSection load='1cj5' size='340' side='right' caption='[[1cj5]], [[NMR_Ensembles_of_Models | 10 NMR models]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cj5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/ | <table><tr><td colspan='2'>[[1cj5]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Bovin Bovin]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1CJ5 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1CJ5 FirstGlance]. <br> | ||
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLG CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">BLG CDNA ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9913 BOVIN])</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=1cj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cj5 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1cj5 RCSB], [http://www.ebi.ac.uk/pdbsum/1cj5 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=1cj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cj5 OCA], [http://pdbe.org/1cj5 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1cj5 RCSB], [http://www.ebi.ac.uk/pdbsum/1cj5 PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | == Function == | ||
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From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | ||
</div> | </div> | ||
<div class="pdbe-citations 1cj5" style="background-color:#fffaf0;"></div> | |||
==See Also== | ==See Also== | ||
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__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[Category: Bovin]] | ||
[[Category: Batt, C A]] | [[Category: Batt, C A]] | ||
[[Category: Era, S]] | [[Category: Era, S]] |
Revision as of 07:47, 10 September 2015
BOVINE BETA-LACTOGLOBULIN ABOVINE BETA-LACTOGLOBULIN A
Structural highlights
Function[LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. 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 PubMedUsing heteronuclear NMR spectroscopy, we studied the solution structure and dynamics of bovine beta-lactoglobulin A at pH 2.0 and 45 degrees C, where the protein exists as a monomeric native state. The monomeric NMR structure, comprising an eight-stranded continuous antiparallel beta-barrel and one major alpha-helix, is similar to the X-ray dimeric structure obtained at pH 6.2, including betaI-strand that forms the dimer interface and loop EF that serves as a lid of the interior hydrophobic hole. [1H]-15N NOE revealed that betaF, betaG, and betaH strands buried under the major alpha-helix are rigid on a pico- to nanosecond time scale and also emphasized rapid fluctuations of loops and the N- and C-terminal regions. Solution structure and dynamics of bovine beta-lactoglobulin A.,Kuwata K, Hoshino M, Forge V, Era S, Batt CA, Goto Y Protein Sci. 1999 Nov;8(11):2541-5. PMID:10595563[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
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