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1mwn
From Proteopedia
| Line 4: | Line 4: | ||
|PDB= 1mwn |SIZE=350|CAPTION= <scene name='initialview01'>1mwn</scene> | |PDB= 1mwn |SIZE=350|CAPTION= <scene name='initialview01'>1mwn</scene> | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene> | + | |LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= S100B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | |GENE= S100B ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY=[[1dt7|1DT7]] | ||
| + | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mwn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mwn OCA], [http://www.ebi.ac.uk/pdbsum/1mwn PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mwn RCSB]</span> | ||
}} | }} | ||
| Line 28: | Line 31: | ||
[[Category: Weber, D J.]] | [[Category: Weber, D J.]] | ||
[[Category: Yang, R.]] | [[Category: Yang, R.]] | ||
| - | [[Category: CA]] | ||
[[Category: 20 structure]] | [[Category: 20 structure]] | ||
[[Category: calcium-binding]] | [[Category: calcium-binding]] | ||
| Line 40: | Line 42: | ||
[[Category: trtk-12]] | [[Category: trtk-12]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:22:13 2008'' |
Revision as of 19:22, 30 March 2008
| |||||||
| Ligands: | |||||||
| Gene: | S100B (Rattus norvegicus) | ||||||
| Related: | 1DT7
| ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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 Sun Mar 30 22:22:13 2008
