This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.

Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


2pru

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px <!-- The line below this paragraph, containing "STRUCTURE_2pru", creates the "Structure Box" on the page. You may change the PDB parameter (which sets the PD...)
Line 1: Line 1:
-
[[Image:2pru.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2pru.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{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==
+
<!--
-
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.
+
The line below this paragraph, {{ABSTRACT_PUBMED_18384084}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 18384084 is the PubMed ID number.
 +
-->
 +
{{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==
Line 30: Line 34:
[[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

Image: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

Page seeded by OCA on Sun Jul 27 17:42:09 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/2pru"
Personal tools