1mwn

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==Overview==
==Overview==
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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.
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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==
==About this Structure==
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[[Category: Protein complex]]
[[Category: Protein complex]]
[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Baldisseri, D.M.]]
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[[Category: Baldisseri, D M.]]
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[[Category: Inman, K.G.]]
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[[Category: Inman, K G.]]
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[[Category: Miller, K.E.]]
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[[Category: Miller, K E.]]
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[[Category: Rustandi, R.R.]]
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[[Category: Rustandi, R R.]]
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[[Category: Weber, D.J.]]
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[[Category: Weber, D J.]]
[[Category: Yang, R.]]
[[Category: Yang, R.]]
[[Category: CA]]
[[Category: CA]]
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[[Category: trtk-12]]
[[Category: trtk-12]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 16:26:07 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:59:53 2008''

Revision as of 11:59, 21 February 2008


1mwn

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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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