View source for 3kza


==Crystal structure of Gyuba, a patched chimera of b-lactglobulin==
<StructureSection load='3kza' size='340' side='right'caption='[[3kza]], [[Resolution|resolution]] 2.00&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[3kza]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus] and [https://en.wikipedia.org/wiki/Equus_caballus Equus caballus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3KZA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3KZA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2&#8491;</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=3kza FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3kza OCA], [https://pdbe.org/3kza PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3kza RCSB], [https://www.ebi.ac.uk/pdbsum/3kza PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3kza 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.[https://www.uniprot.org/uniprot/LACB1_HORSE LACB1_HORSE] Lactoglobulin is the primary component of whey, it binds retinol and is probably involved in the transport of that molecule.
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
beta-lactoglobulin (LG) contains nine beta-strands (strands A-I) and one alpha-helix. Strands A-H form a beta-barrel. At neutral pH, equine LG (ELG) is monomeric, whereas bovine LG (BLG) is dimeric, and the I-strands of its two subunits form an intermolecular beta-sheet. We previously constructed a chimeric ELG in which the sequence of the I-strand was replaced with that of BLG. This chimera did not dimerize. For this study, we constructed the new chimera we call Gyuba (which means cow and horse in Japanese). The amino acid sequence of Gyuba includes the sequences of the BLG secondary structures and those of the ELG loops. The crystal structure of Gyuba is very similar to that of BLG and indicates that Gyuba dimerizes via the intermolecular beta-sheet formed by the two I-strands. Thus, the entire arrangement of the secondary structural elements is important for LG dimer formation.

Structure and stability of Gyuba, a beta-lactoglobulin chimera.,Ohtomo H, Konuma T, Utsunoiya H, Tsuge H, Ikeguchi M Protein Sci. 2011 Nov;20(11):1867-75. doi: 10.1002/pro.720. Epub 2011 Sep, 22. PMID:21853497<ref>PMID:21853497</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 3kza" style="background-color:#fffaf0;"></div>

==See Also==
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Bos taurus]]
[[Category: Equus caballus]]
[[Category: Large Structures]]
[[Category: Ikeguchi M]]
[[Category: Konuma T]]
[[Category: Ohtomo H]]
[[Category: Tsuge H]]
[[Category: Utsunomiya H]]