1mq1

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[[Image:1mq1.jpg|left|200px]]
[[Image:1mq1.jpg|left|200px]]
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{{Structure
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|GENE= S100beta ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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{{STRUCTURE_1mq1| PDB=1mq1 | SCENE= }}
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|RELATEDENTRY=[[1uwo|1UWO]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1mq1 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1mq1 OCA], [http://www.ebi.ac.uk/pdbsum/1mq1 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1mq1 RCSB]</span>
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'''Ca2+-S100B-TRTK-12 complex'''
'''Ca2+-S100B-TRTK-12 complex'''
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[[Category: McClintock, K A.]]
[[Category: McClintock, K A.]]
[[Category: Shaw, G S.]]
[[Category: Shaw, G S.]]
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[[Category: ef-hand]]
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[[Category: Ef-hand]]
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[[Category: protein-peptide complex]]
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[[Category: Protein-peptide complex]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 01:34:47 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:19:35 2008''
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Revision as of 22:34, 2 May 2008

Template:STRUCTURE 1mq1

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 Page seeded by OCA on Sat May 3 01:34:47 2008

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