1cj5: Difference between revisions
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< | ==BOVINE BETA-LACTOGLOBULIN A== | ||
<StructureSection load='1cj5' size='340' side='right'caption='[[1cj5]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cj5]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. 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 [https://proteopedia.org/fgij/fg.htm?mol=1CJ5 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 10 models</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=1cj5 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1cj5 OCA], [https://pdbe.org/1cj5 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1cj5 RCSB], [https://www.ebi.ac.uk/pdbsum/1cj5 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1cj5 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/LACB_BOVIN LACB_BOVIN] Primary component of whey, it binds retinol and is probably involved in the transport of that molecule. | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/1cj5_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1cj5 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Using 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<ref>PMID:10595563</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1cj5" style="background-color:#fffaf0;"></div> | |||
==See Also== | |||
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
== | |||
== | |||
< | |||
[[Category: Bos taurus]] | [[Category: Bos taurus]] | ||
[[Category: Batt | [[Category: Large Structures]] | ||
[[Category: Era | [[Category: Batt CA]] | ||
[[Category: Forge | [[Category: Era S]] | ||
[[Category: Goto | [[Category: Forge V]] | ||
[[Category: Hoshino | [[Category: Goto Y]] | ||
[[Category: Kuwata | [[Category: Hoshino M]] | ||
[[Category: Kuwata K]] | |||
Latest revision as of 23:52, 20 November 2024
BOVINE BETA-LACTOGLOBULIN A
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