1mwn
From Proteopedia
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'''Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12''' | '''Solution NMR structure of S100B bound to the high-affinity target peptide TRTK-12''' | ||
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[[Category: Yang, R.]] | [[Category: Yang, R.]] | ||
[[Category: 20 structure]] | [[Category: 20 structure]] | ||
- | [[Category: | + | [[Category: Calcium-binding]] |
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- | [[Category: | + | [[Category: Four helix bundle]] |
- | [[Category: | + | [[Category: Helix loop helix]] |
- | [[Category: | + | [[Category: Nmr]] |
- | [[Category: | + | [[Category: Protein-peptide complex]] |
- | [[Category: | + | [[Category: S100 protein]] |
- | [[Category: | + | [[Category: S100b]] |
- | [[Category: | + | [[Category: Trtk-12]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:48:37 2008'' | |
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Revision as of 22:48, 2 May 2008
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. 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 Page seeded by OCA on Sat May 3 01:48:37 2008