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1jss

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(New page: 200px<br /><applet load="1jss" size="450" color="white" frame="true" align="right" spinBox="true" caption="1jss, resolution 2.20&Aring;" /> '''Crystal structure of...)
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[[Image:1jss.gif|left|200px]]<br /><applet load="1jss" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1jss.gif|left|200px]]<br /><applet load="1jss" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1jss, resolution 2.20&Aring;" />
caption="1jss, resolution 2.20&Aring;" />
'''Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4).'''<br />
'''Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4).'''<br />
==Overview==
==Overview==
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The x-ray structure of the mouse cholesterol-regulated START protein 4, (StarD4) has been determined at 2.2-A resolution, revealing a compact, alpha/beta structure related to the START domain present in the, cytoplasmic C-terminal portion of human MLN64. The volume of the putative, lipid-binding tunnel was estimated at 847 A(3), which is consistent with, the binding of one cholesterol-size lipid molecule. Comparison of the, tunnel-lining residues in StarD4 and MLN64-START permitted identification, of possible lipid specificity determinants in both molecular tunnels., Homology modeling of related proteins, and comparison of the StarD4 and, MLN64-START structures, showed that StarD4 is a member of a large START, domain superfamily characterized by the helix-grip fold. Additional, mechanistic and evolutionary studies should be facilitated by the, availability of a second START domain structure from a distant relative of, MLN64.
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The x-ray structure of the mouse cholesterol-regulated START protein 4 (StarD4) has been determined at 2.2-A resolution, revealing a compact alpha/beta structure related to the START domain present in the cytoplasmic C-terminal portion of human MLN64. The volume of the putative lipid-binding tunnel was estimated at 847 A(3), which is consistent with the binding of one cholesterol-size lipid molecule. Comparison of the tunnel-lining residues in StarD4 and MLN64-START permitted identification of possible lipid specificity determinants in both molecular tunnels. Homology modeling of related proteins, and comparison of the StarD4 and MLN64-START structures, showed that StarD4 is a member of a large START domain superfamily characterized by the helix-grip fold. Additional mechanistic and evolutionary studies should be facilitated by the availability of a second START domain structure from a distant relative of MLN64.
==About this Structure==
==About this Structure==
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1JSS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1JSS OCA].
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1JSS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Mus_musculus Mus musculus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1JSS OCA].
==Reference==
==Reference==
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[[Category: Mus musculus]]
[[Category: Mus musculus]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Breslow, J.L.]]
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[[Category: Breslow, J L.]]
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[[Category: Burley, S.K.]]
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[[Category: Burley, S K.]]
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[[Category: NYSGXRC, New.York.Structural.GenomiX.Research.Consortium.]]
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[[Category: NYSGXRC, New York Structural GenomiX Research Consortium.]]
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[[Category: Romanowski, M.J.]]
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[[Category: Romanowski, M J.]]
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[[Category: Soccio, R.E.]]
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[[Category: Soccio, R E.]]
[[Category: new york structural genomix research consortium]]
[[Category: new york structural genomix research consortium]]
[[Category: nysgxrc]]
[[Category: nysgxrc]]
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[[Category: structural genomics]]
[[Category: structural genomics]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 18:32:53 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:26:23 2008''

Revision as of 11:26, 21 February 2008


1jss, resolution 2.20Å

Drag the structure with the mouse to rotate

Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4).

Overview

The x-ray structure of the mouse cholesterol-regulated START protein 4 (StarD4) has been determined at 2.2-A resolution, revealing a compact alpha/beta structure related to the START domain present in the cytoplasmic C-terminal portion of human MLN64. The volume of the putative lipid-binding tunnel was estimated at 847 A(3), which is consistent with the binding of one cholesterol-size lipid molecule. Comparison of the tunnel-lining residues in StarD4 and MLN64-START permitted identification of possible lipid specificity determinants in both molecular tunnels. Homology modeling of related proteins, and comparison of the StarD4 and MLN64-START structures, showed that StarD4 is a member of a large START domain superfamily characterized by the helix-grip fold. Additional mechanistic and evolutionary studies should be facilitated by the availability of a second START domain structure from a distant relative of MLN64.

About this Structure

1JSS is a Single protein structure of sequence from Mus musculus. Full crystallographic information is available from OCA.

Reference

Crystal structure of the Mus musculus cholesterol-regulated START protein 4 (StarD4) containing a StAR-related lipid transfer domain., Romanowski MJ, Soccio RE, Breslow JL, Burley SK, Proc Natl Acad Sci U S A. 2002 May 14;99(10):6949-54. PMID:12011453

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