1mq1: Difference between revisions
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'''Ca2+-S100B-TRTK-12 complex''' | {{Structure | ||
|PDB= 1mq1 |SIZE=350|CAPTION= <scene name='initialview01'>1mq1</scene> | |||
|SITE= | |||
|LIGAND= | |||
|ACTIVITY= | |||
|GENE= S100beta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens]) | |||
}} | |||
'''Ca2+-S100B-TRTK-12 complex''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1MQ1 is a [ | 1MQ1 is a [[Protein complex]] structure of sequences from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1MQ1 OCA]. | ||
==Reference== | ==Reference== | ||
A novel S100 target conformation is revealed by the solution structure of the Ca2+-S100B-TRTK-12 complex., McClintock KA, Shaw GS, J Biol Chem. 2003 Feb 21;278(8):6251-7. Epub 2002 Dec 11. PMID:[http:// | A novel S100 target conformation is revealed by the solution structure of the Ca2+-S100B-TRTK-12 complex., McClintock KA, Shaw GS, J Biol Chem. 2003 Feb 21;278(8):6251-7. Epub 2002 Dec 11. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12480931 12480931] | ||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: Protein complex]] | [[Category: Protein complex]] | ||
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[[Category: protein-peptide complex]] | [[Category: protein-peptide complex]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:46:43 2008'' | ||
Revision as of 10:46, 20 March 2008
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| Gene: | S100beta (Homo sapiens) | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
Ca2+-S100B-TRTK-12 complex
Overview
The Alzheimer-linked neural protein S100B is a signaling molecule shown to control the assembly of intermediate filament proteins in a calcium-sensitive manner. Upon binding calcium, a conformational change occurs in S100B exposing a hydrophobic surface for target protein interactions. The synthetic peptide TRTK-12 (TRTKIDWNKILS), derived from random bacteriophage library screening, bears sequence similarity to several intermediate filament proteins and has the highest calcium-dependent affinity of any target molecule for S100B to date (K(d) <1 microm). In this work, the three-dimensional structure of the Ca(2+)-S100B-TRTK-12 complex has been determined by NMR spectroscopy. The structure reveals an extended, contiguous hydrophobic surface is formed on Ca(2+)-S100B for target interaction. The TRTK-12 peptide adopts a coiled structure that fits into a portion of this surface, anchored at Trp(7), and interacts with multiple hydrophobic contacts in helices III and IV of Ca(2+)-S100B. This interaction is strikingly different from the alpha-helical structures found for other S100 target peptides. By using the TRTK-12 interaction as a guide, in combination with other available S100 target structures, a recognition site on helix I is identified that may act in concert with the TRTK-12-binding site from helices III and IV. This would provide a larger, more complex site to interact with full-length target proteins and would account for the promiscuity observed for S100B target protein interactions.
About this Structure
1MQ1 is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.
Reference
A novel S100 target conformation is revealed by the solution structure of the Ca2+-S100B-TRTK-12 complex., McClintock KA, Shaw GS, J Biol Chem. 2003 Feb 21;278(8):6251-7. Epub 2002 Dec 11. PMID:12480931
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