1mwn
From Proteopedia
(New page: 200px<br /> <applet load="1mwn" size="450" color="white" frame="true" align="right" spinBox="true" caption="1mwn" /> '''Solution NMR structure of S100B bound to th...) |
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'''Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12'''<br /> | '''Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1MWN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1MWN is a [http://en.wikipedia.org/wiki/Protein_complex Protein complex] structure of sequences from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MWN OCA]. |
==Reference== | ==Reference== | ||
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[[Category: trtk-12]] | [[Category: trtk-12]] | ||
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Revision as of 14:26, 15 February 2008
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Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12
Overview
The solution NMR structure is reported for Ca(2+)-loaded S100B bound to a, 12-residue peptide, TRTK-12, from the actin capping protein CapZ (alpha1, or alpha2 subunit, residues 265-276: TRTKIDWNKILS). This peptide was, discovered by Dimlich and co-workers by screening a bacteriophage random, peptide display library, and it matches exactly the consensus S100B, binding sequence ((K/R)(L/I)XWXXIL). As with other S100B target proteins, a calcium-dependent conformational change in S100B is required for TRTK-12, binding. The TRTK-12 peptide is an amphipathic helix (residues W7 to S12), in the S100B-TRTK complex, and helix 4 of S100B is extended by three or, four residues upon peptide binding. However, helical TRTK-12 in the, S100B-peptide complex is uniquely oriented when compared to the, three-dimensional structures of other S100-peptide complexes. The, three-dimensional structure of the S100B-TRTK peptide complex illustrates, that residues in the S100B binding consensus sequence (K4, I5, W7, I10, L11) are all involved in the S100B-peptide interface, which can explain, its orientation in the S100B binding pocket and its relatively high, binding affinity. A comparison of the S100B-TRTK peptide structure to the, structures of apo- and Ca(2+)-bound S100B illustrates that the binding, site of TRTK-12 is buried in apo-S100B, but is exposed in Ca(2+)-bound, S100B as necessary to bind the TRTK-12 peptide.
About this Structure
1MWN is a Protein complex structure of sequences from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12., Inman KG, Yang R, Rustandi RR, Miller KE, Baldisseri DM, Weber DJ, J Mol Biol. 2002 Dec 13;324(5):1003-14. PMID:12470955
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