1b4c

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|ACTIVITY=
|ACTIVITY=
|GENE= S100BETA FROM RATTUS NORVEGICUS (RAT) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
|GENE= S100BETA FROM RATTUS NORVEGICUS (RAT) ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus])
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|RELATEDENTRY=
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|RESOURCES=<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.ebi.ac.uk/pdbsum/1b4c PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1b4c RCSB]</span>
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[[Category: three-dimensional structure]]
[[Category: three-dimensional structure]]
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Revision as of 15:53, 30 March 2008


PDB ID 1b4c

Drag the structure with the mouse to rotate
Gene: S100BETA FROM RATTUS NORVEGICUS (RAT) (Rattus norvegicus)
Resources: FirstGlance, OCA, PDBsum, RCSB
Coordinates: save as pdb, mmCIF, xml



SOLUTION STRUCTURE OF RAT APO-S100B USING DIPOLAR COUPLINGS


Overview

The 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.

About this Structure

1B4C is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.

Reference

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

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