1b4c: Difference between revisions
No edit summary |
No edit summary |
||
| Line 3: | Line 3: | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1b4c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B4C FirstGlance]. <br> | <table><tr><td colspan='2'>[[1b4c]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1B4C OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1B4C FirstGlance]. <br> | ||
</td></tr><tr><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICUS (RAT) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</td></tr> | </td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">S100BETA FROM RATTUS NORVEGICUS (RAT) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])</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=1b4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b4c RCSB], [http://www.ebi.ac.uk/pdbsum/1b4c PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1b4c FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1b4c OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1b4c RCSB], [http://www.ebi.ac.uk/pdbsum/1b4c PDBsum]</span></td></tr> | ||
<table> | </table> | ||
== Evolutionary Conservation == | == Evolutionary Conservation == | ||
[[Image:Consurf_key_small.gif|200px|right]] | [[Image:Consurf_key_small.gif|200px|right]] | ||
| Line 32: | Line 32: | ||
</StructureSection> | </StructureSection> | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Baldisseri, D M | [[Category: Baldisseri, D M]] | ||
[[Category: Drohat, A C | [[Category: Drohat, A C]] | ||
[[Category: Tjandra, N | [[Category: Tjandra, N]] | ||
[[Category: Weber, D J | [[Category: Weber, D J]] | ||
[[Category: Calcium- binding protein]] | [[Category: Calcium- binding protein]] | ||
[[Category: Dipolar coupling]] | [[Category: Dipolar coupling]] | ||
Revision as of 12:22, 22 December 2014
SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGSSOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS
Structural highlights
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 PubMedThe relative orientations of adjacent structural elements without many well-defined NOE contacts between them are typically poorly defined in NMR structures. For apo-S100B(betabeta) and the structurally homologous protein calcyclin, the solution structures determined by conventional NMR exhibited considerable differences and made it impossible to draw unambiguous conclusions regarding the Ca2+-induced conformational change required for target protein binding. The structure of rat apo-S100B(betabeta) was recalculated using a large number of constraints derived from dipolar couplings that were measured in a dilute liquid crystalline phase. The dipolar couplings orient bond vectors relative to a single-axis system, and thereby remove much of the uncertainty in NOE-based structures. The structure of apo-S100B(betabeta) indicates a minimal change in the first, pseudo-EF-hand Ca2+ binding site, but a large reorientation of helix 3 in the second, classical EF-hand upon Ca2+ binding. The use of dipolar couplings for determining the solution structure of rat apo-S100B(betabeta).,Drohat AC, Tjandra N, Baldisseri DM, Weber DJ Protein Sci. 1999 Apr;8(4):800-9. PMID:10211826[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences |
| ||||||||||||||||