1cj5: Difference between revisions
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==BOVINE BETA-LACTOGLOBULIN A== | ==BOVINE BETA-LACTOGLOBULIN A== | ||
<StructureSection load='1cj5' size='340' side='right' caption='[[1cj5 | <StructureSection load='1cj5' size='340' side='right'caption='[[1cj5]]' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1cj5]] is a 1 chain structure with sequence from [ | <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=' | </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'>[ | <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> | </table> | ||
== Function == | == 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 == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
Check<jmol> | Check<jmol> | ||
<jmolCheckbox> | <jmolCheckbox> | ||
<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/cj/1cj5_consurf.spt"</scriptWhenChecked> | <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/ | <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview03.spt</scriptWhenUnchecked> | ||
<text>to colour the structure by Evolutionary Conservation</text> | <text>to colour the structure by Evolutionary Conservation</text> | ||
</jmolCheckbox> | </jmolCheckbox> | ||
| Line 29: | Line 30: | ||
==See Also== | ==See Also== | ||
*[[Beta-lactoglobulin|Beta-lactoglobulin]] | *[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]] | ||
== References == | == References == | ||
<references/> | <references/> | ||
__TOC__ | __TOC__ | ||
</StructureSection> | </StructureSection> | ||
[[Category: | [[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 02:52, 21 November 2024
BOVINE BETA-LACTOGLOBULIN ABOVINE BETA-LACTOGLOBULIN A
Structural highlights
FunctionLACB_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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