1exs

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Current revision (08:25, 6 November 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
{{Seed}}
 
-
[[Image:1exs.png|left|200px]]
 
-
<!--
+
==STRUCTURE OF PORCINE BETA-LACTOGLOBULIN==
-
The line below this paragraph, containing "STRUCTURE_1exs", creates the "Structure Box" on the page.
+
<StructureSection load='1exs' size='340' side='right'caption='[[1exs]], [[Resolution|resolution]] 2.39&Aring;' scene=''>
-
You may change the PDB parameter (which sets the PDB file loaded into the applet)
+
== Structural highlights ==
-
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
+
<table><tr><td colspan='2'>[[1exs]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXS OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1EXS FirstGlance]. <br>
-
or leave the SCENE parameter empty for the default display.
+
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.39&#8491;</td></tr>
-
-->
+
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=NA:SODIUM+ION'>NA</scene></td></tr>
-
{{STRUCTURE_1exs| PDB=1exs | SCENE= }}
+
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1exs FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1exs OCA], [https://pdbe.org/1exs PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1exs RCSB], [https://www.ebi.ac.uk/pdbsum/1exs PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1exs ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/LACB_PIG LACB_PIG] Lactoglobulin is the 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/ex/1exs_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=1exs ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
beta-Lactoglobulin (BLG) is a lipocalin and is the major protein in the whey of the milk of cows and other ruminants, but not in all mammalian species. The biological function of BLG is not clear, but a potential role in carrying fatty acids through the digestive tract has been proposed. The capability of BLG to aggregate and form gels is often used to thicken foodstuffs. The structure of the porcine form is sufficiently different from other known BLG structures that SIRAS phases had to be measured in order to solve the crystal structure to 2.4 A resolution. The r.m.s. deviation of C(alpha) atoms is 2.8 A between porcine and bovine BLG. Nevertheless, the typical lipocalin fold is conserved. Compared with bovine BLG, the tilted alpha-helix alters the arrangement of surface residues of the porcine form, completely changing the dimerization behaviour. Through a unique pH-dependent domain-swapping mechanism involving the first ten residues, a novel dimer interface is formed at the N-terminus of porcine BLG. The existence of this novel dimer at low pH is supported by gel-filtration experiments. These results provide a rationale for the difference in physicochemical behaviour between bovine and porcine BLG and point the way towards engineering such dimerization motifs into other members of the lipocalin family.
-
===STRUCTURE OF PORCINE BETA-LACTOGLOBULIN===
+
A novel pH-dependent dimerization motif in beta-lactoglobulin from pig (Sus scrofa).,Hoedemaeker FJ, Visschers RW, Alting AC, de Kruif KG, Kuil ME, Abrahams JP Acta Crystallogr D Biol Crystallogr. 2002 Mar;58(Pt 3):480-6. Epub 2002, Feb 21. PMID:11856834<ref>PMID:11856834</ref>
 +
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
 +
</div>
 +
<div class="pdbe-citations 1exs" style="background-color:#fffaf0;"></div>
-
<!--
+
==See Also==
-
The line below this paragraph, {{ABSTRACT_PUBMED_11856834}}, adds the Publication Abstract to the page
+
*[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
-
(as it appears on PubMed at http://www.pubmed.gov), where 11856834 is the PubMed ID number.
+
== References ==
-
-->
+
<references/>
-
{{ABSTRACT_PUBMED_11856834}}
+
__TOC__
-
 
+
</StructureSection>
-
==About this Structure==
+
[[Category: Large Structures]]
-
1EXS is a 1 chain structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1EXS OCA].
+
-
 
+
-
==Reference==
+
-
<ref group="xtra">PMID:11856834</ref><references group="xtra"/>
+
[[Category: Sus scrofa]]
[[Category: Sus scrofa]]
-
[[Category: Abrahams, J P.]]
+
[[Category: Abrahams JP]]
-
[[Category: Hoedemaeker, F J.]]
+
[[Category: Hoedemaeker FJ]]
-
[[Category: Lipocalin fold]]
+
-
 
+
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 04:54:21 2009''
+

Current revision

STRUCTURE OF PORCINE BETA-LACTOGLOBULIN

PDB ID 1exs

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1exs"
Personal tools