2nln
From Proteopedia
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| - | [[Image:2nln.jpg|left|200px]] | + | [[Image:2nln.jpg|left|200px]] |
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| - | '''Solution Structure of Calcium-free Rat Beta-parvalbumin''' | + | {{Structure |
| + | |PDB= 2nln |SIZE=350|CAPTION= <scene name='initialview01'>2nln</scene> | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= Ocm ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Rattus norvegicus]) | ||
| + | }} | ||
| + | |||
| + | '''Solution Structure of Calcium-free Rat Beta-parvalbumin''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 2NLN is a [ | + | 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]. |
==Reference== | ==Reference== | ||
| - | Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin)., Henzl MT, Tanner JJ, Protein Sci. 2007 Sep;16(9):1914-26. PMID:[http:// | + | Solution structure of Ca2+-free rat beta-parvalbumin (oncomodulin)., Henzl MT, Tanner JJ, Protein Sci. 2007 Sep;16(9):1914-26. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17766386 17766386] |
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: rat oncomodulin]] | [[Category: rat oncomodulin]] | ||
| - | ''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 17:48:03 2008'' |
Revision as of 15:48, 20 March 2008
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| Gene: | Ocm (Rattus norvegicus) | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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.
About this Structure
2NLN is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic 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 Thu Mar 20 17:48:03 2008
