1dv9: Difference between revisions

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 ==STRUCTURAL CHANGES ACCOMPANYING PH-INDUCED DISSOCIATION OF THE B-LACTOGLOBULIN DIMER==
-<StructureSection load='1dv9' size='340' side='right'caption='[[1dv9]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>
+<StructureSection load='1dv9' size='340' side='right'caption='[[1dv9]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1dv9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Bovin Bovin]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1DV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DV9 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1dv9]] 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=1DV9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1DV9 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1bsy|1bsy]], [[2blg|2blg]], [[3blg|3blg]], [[1b0o|1b0o]], [[1beb|1beb]], [[1bso|1bso]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1dv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dv9 OCA], [https://pdbe.org/1dv9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1dv9 RCSB], [https://www.ebi.ac.uk/pdbsum/1dv9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1dv9 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/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]]
@@ Line 19: / Line 19: @@
 </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=1dv9 ConSurf].
 <div style="clear:both"></div>
-<div style="background-color:#fffaf0;">
-== Publication Abstract from PubMed ==
-We have used NMR spectroscopy to determine the three-dimensional (3D) structure, and to characterize the backbone dynamics, of a recombinant version of bovine beta-lactoglobulin (variant A) at pH 2. 6, where the protein is a monomer. The structure of this low-pH form of beta-lactoglobulin is very similar to that of a subunit within the dimer at pH 6.2. The root-mean-square deviation from the pH 6.2 (crystal) structure, calculated for backbone atoms of residues 6-160, is approximately 1.3 A. Differences arise from the orientation, with respect to the calyx, of the A-B and C-D loops, and of the flanking three-turn alpha-helix. The hydrophobic cavity within the calyx is retained at low pH. The E-F loop (residues 85-90), which moves to occlude the opening of the cavity over the pH range 7.2-6.2, is in the "closed" position at pH 2.6, and the side chain of Glu89 is buried. We also carried out measurements of (15)N T(1)s and T(2)s and (1)H-(15)N heteronuclear NOEs at pH 2.6 and 37 degrees C. Although the residues of the E-F loop (residues 86-89) have the highest crystallographic B-factors, the conformation of this loop is reasonably well defined by the NMR data, and its backbone is not especially mobile on the pico- to nanosecond time scale. Several residues (Ser21, Lys60, Ala67, Leu87, and Glu112) exhibit large ratios of T(1) to T(2), consistent with conformational exchange on a micro- to millisecond time scale. The positions of these residues in the 3D structure of beta-lactoglobulin are consistent with a role in modulating access to the hydrophobic cavity.
-Structural changes accompanying pH-induced dissociation of the beta-lactoglobulin dimer.,Uhrinova S, Smith MH, Jameson GB, Uhrin D, Sawyer L, Barlow PN Biochemistry. 2000 Apr 4;39(13):3565-74. PMID:10736155<ref>PMID:10736155</ref>
-From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-</div>
-<div class="pdbe-citations 1dv9" style="background-color:#fffaf0;"></div>
 ==See Also==
 *[[Beta-lactoglobulin 3D structures|Beta-lactoglobulin 3D structures]]
-== References ==
-<references/>
 __TOC__
 </StructureSection>
-[[Category: Bovin]]
+[[Category: Bos taurus]]
 [[Category: Large Structures]]
-[[Category: Barlow, P N]]
+[[Category: Barlow PN]]
-[[Category: Jameson, G B]]
+[[Category: Jameson GB]]
-[[Category: Sawyer, L]]
+[[Category: Sawyer L]]
-[[Category: Smith, M H]]
+[[Category: Smith MH]]
-[[Category: Uhrin, D]]
+[[Category: Uhrin D]]
-[[Category: Uhrinova, S]]
+[[Category: Uhrinova S]]
-[[Category: Beta-barrel]]
-[[Category: Beta-lactoglobulin]]
-[[Category: Low ph structure]]
-[[Category: Transport protein]]
-[[Category: Triple resonance experiment]]