2pru: Difference between revisions

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[[Image:2pru.jpg|left|200px]]
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{{STRUCTURE_2pru|  PDB=2pru  |  SCENE=  }}  
{{STRUCTURE_2pru|  PDB=2pru  |  SCENE=  }}  


'''NMR Structure of Human apoS100B at 10C'''
===NMR Structure of Human apoS100B at 10C===




==Overview==
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S100B is one of the best-characterized members of the calcium-signaling S100 protein family. Most S100 proteins are dimeric, with each monomer containing two EF-hand calcium-binding sites (EF1, EF2). S100B and other S100 proteins respond to calcium increases in the cell by coordinating calcium and undergoing a conformational change that allows them to interact with a variety of cellular targets. Although several three dimensional structures of S100 proteins are available in the calcium-free (apo-) state it has been observed that these structures appear to adopt a wide range of conformations in the EF2 site with respect to the positioning of helix III, the helix that undergoes the most dramatic calcium-induced conformational change. In this work, we have determined the structure of human apo-S100B at 10 degrees C to examine whether temperature might be responsible for these structural differences. Further, we have used this data, and other available apo-S100 structures, to show that despite the range of interhelical angles adopted in the apo-S100 structures, normal Gaussian distributions about the mean angles found in the structure of human apo-S100B are observed. This finding, only obvious from the analysis of all available apo-S100 proteins, provides direct structural evidence that helix III is a loosely packed helix. This is likely a necessary functional property of the S100 proteins that facilitates the calcium-induced conformational change of helix III. In contrast, the calcium-bound structures of the S100 proteins show significantly smaller variability in the interhelical angles. This shows that calcium binding to the S100 proteins causes not only a conformational change but results in a tighter distribution of helices within the EF2 calcium binding site required for target protein interactions. Proteins 2008. (c) 2008 Wiley-Liss, Inc.
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{{ABSTRACT_PUBMED_18384084}}


==About this Structure==
==About this Structure==
2PRU is a [[Single protein]] structure of sequence 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=2PRU OCA].  
2PRU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2PRU OCA].  


==Reference==
==Reference==
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[[Category: Metal binding protein]]
[[Category: Metal binding protein]]
[[Category: S100]]
[[Category: S100]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Apr 16 23:04:09 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 17:42:09 2008''

Revision as of 14:42, 27 July 2008

File:2pru.png

Template:STRUCTURE 2pru

NMR Structure of Human apoS100B at 10C

Template:ABSTRACT PUBMED 18384084

About this Structure

2PRU is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Analysis of the structure of human apo-S100B at low temperature indicates a unimodal conformational distribution is adopted by calcium-free S100 proteins., Malik S, Revington M, Smith SP, Shaw GS, Proteins. 2008 Apr 2;. PMID:18384084

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