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.


2nln

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:2nln.jpg|left|200px]]
+
{{Seed}}
 +
[[Image:2nln.png|left|200px]]
<!--
<!--
Line 9: Line 10:
{{STRUCTURE_2nln| PDB=2nln | SCENE= }}
{{STRUCTURE_2nln| PDB=2nln | SCENE= }}
-
'''Solution Structure of Calcium-free Rat Beta-parvalbumin'''
+
===Solution Structure of Calcium-free Rat Beta-parvalbumin===
-
==Overview==
+
<!--
-
Relative to other parvalbumin isoforms, the mammalian beta-parvalbumin (oncomodulin) displays attenuated divalent ion affinity. High-resolution structural data for the Ca(2+)-bound protein have provided little insight into the physical basis for this behavior, prompting an examination of the unliganded state. This article describes the solution structure and peptide backbone dynamics of Ca(2+)-free rat beta-parvalbumin (beta-PV). Ca(2+) removal evidently provokes significant structural alterations. Interaction between the D helix and the AB domain in the Ca(2+)-bound protein is greatly diminished in the apo-form, permitting the D helix to straighten. There is also a significant reorganization of the hydrophobic core and a concomitant remodeling of the interface between the AB and CD-EF domains. These modifications perturb the orientation of the C and D helices, and the energetic penalty associated with their reversal could contribute to the low-affinity signature of the CD site. By contrast, Ca(2+) removal causes a comparatively minor perturbation of the E and F helices, consistent with the more typical divalent ion affinity observed for the EF site. Ca(2+)-free rat beta-PV retains structural rigidity on the picosecond-nanosecond timescale. At 20 degrees C, the majority of amide vectors show no evidence for motion on timescales above 20 ps, and the average order parameter for the entire molecule is 0.92.
+
The line below this paragraph, {{ABSTRACT_PUBMED_17766386}}, adds the Publication Abstract to the page
 +
(as it appears on PubMed at http://www.pubmed.gov), where 17766386 is the PubMed ID number.
 +
-->
 +
{{ABSTRACT_PUBMED_17766386}}
==About this Structure==
==About this Structure==
-
2NLN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NLN OCA].
+
2NLN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2NLN OCA].
==Reference==
==Reference==
Line 27: Line 31:
[[Category: Rat beta parvalbumin]]
[[Category: Rat beta parvalbumin]]
[[Category: Rat oncomodulin]]
[[Category: Rat oncomodulin]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 09:36:57 2008''
+
 
 +
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 14:52:17 2008''

Revision as of 11:52, 28 July 2008

Image:2nln.png

Template:STRUCTURE 2nln

Solution Structure of Calcium-free Rat Beta-parvalbumin

Template:ABSTRACT PUBMED 17766386

About this Structure

2NLN is a Single protein structure of sequence from Rattus norvegicus. Full experimental information is available from OCA.

Reference

Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin)., Henzl MT, Tanner JJ, Protein Sci. 2007 Sep;16(9):1914-26. PMID:17766386

Page seeded by OCA on Mon Jul 28 14:52:17 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

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