1dv9

<StructureSection load='1dv9' size='340' side='right' caption='[[1dv9]], [[NMR_Ensembles_of_Models | 21 NMR models]]' scene=''>

<table><tr><td colspan='2'>[[1dv9]] is a 1 chain structure with sequence from [http://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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1DV9 FirstGlance]. <br>

</td></tr><tr><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1bsy|1bsy]], [[2blg|2blg]], [[3blg|3blg]], [[1b0o|1b0o]], [[1beb|1beb]], [[1bso|1bso]]</td></tr>

<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1dv9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1dv9 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1dv9 RCSB], [http://www.ebi.ac.uk/pdbsum/1dv9 PDBsum]</span></td></tr>

<table>

<scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/dv/1dv9_consurf.spt"</scriptWhenChecked>

</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/chain_selection.php?pdb_ID=2ata ConSurf].

<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>

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*[[Beta-lactoglobulin|Beta-lactoglobulin]]

[[Category: Barlow, P N.]]

[[Category: Jameson, G B.]]

[[Category: Sawyer, L.]]

[[Category: Smith, M H.]]

[[Category: Uhrin, D.]]

[[Category: Uhrinova, S.]]

[[Category: Triple resonance experiment]]