1jdm

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[[Image:1jdm.gif|left|200px]]<br /><applet load="1jdm" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jdm.gif|left|200px]]
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caption="1jdm" />
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'''NMR Structure of Sarcolipin'''<br />
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{{Structure
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|PDB= 1jdm |SIZE=350|CAPTION= <scene name='initialview01'>1jdm</scene>
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|SITE=
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|LIGAND=
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|ACTIVITY=
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|GENE=
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}}
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'''NMR Structure of Sarcolipin'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1JDM is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDM OCA].
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1JDM is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ ]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JDM OCA].
==Reference==
==Reference==
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Structure and orientation of sarcolipin in lipid environments., Mascioni A, Karim C, Barany G, Thomas DD, Veglia G, Biochemistry. 2002 Jan 15;41(2):475-82. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11781085 11781085]
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Structure and orientation of sarcolipin in lipid environments., Mascioni A, Karim C, Barany G, Thomas DD, Veglia G, Biochemistry. 2002 Jan 15;41(2):475-82. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/11781085 11781085]
[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Mascioni, A.]]
[[Category: Mascioni, A.]]
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[[Category: helix]]
[[Category: helix]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:21:26 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:01:58 2008''

Revision as of 10:01, 20 March 2008


PDB ID 1jdm

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NMR Structure of Sarcolipin


Overview

Sarcolipin (SLN) is a 31 amino acid integral membrane protein that regulates Ca-ATPase activity in skeletal muscle. Here, we report the three-dimensional structure and topology of synthetic SLN in lipid environments, as determined by solution and solid-state NMR spectroscopy. 2D solution NMR experiments were performed on SLN solubilized in sodium dodecyl sulfate (SDS) micelles. We found that SLN adopts a highly defined alpha-helical conformation from F9 through R27, with a backbone RMSD of 0.65 A and a side chain RMSD of 1.66 A. The N-terminus (M1 through L8) and the C-terminus (S28 through Y31) are mostly unstructured. The orientation of the SLN was determined using one-dimensional (15)N NMR solid-state spectroscopy. The protein was incorporated into phospholipid bilayers prepared from a mixture of 1,2-dioleoyl-sn-glycero-3-phosphocholine and 1,2-dioleoyl-sn-glycero-3-phosphoethanolamine. The (15)N chemical shift solid-state spectra from selectively labeled SLN samples indicate that SLN orients perpendicularly to the plane of the membrane bilayers. These results support the proposed mechanism of Ca-ATPase regulation of SLN via protein-protein intramembranous interactions between the highly conserved transmembrane domains of the Ca-ATPase and the conserved transmembrane domain of SLN.

About this Structure

1JDM is a Single protein structure of sequence from [1]. Full crystallographic information is available from OCA.

Reference

Structure and orientation of sarcolipin in lipid environments., Mascioni A, Karim C, Barany G, Thomas DD, Veglia G, Biochemistry. 2002 Jan 15;41(2):475-82. PMID:11781085

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