1hek

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(New page: 200px<br /><applet load="1hek" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hek, resolution 2.80&Aring;" /> '''CRYSTAL STRUCTURE OF...)
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[[Image:1hek.gif|left|200px]]<br /><applet load="1hek" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1hek.gif|left|200px]]<br /><applet load="1hek" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1hek, resolution 2.80&Aring;" />
caption="1hek, resolution 2.80&Aring;" />
'''CRYSTAL STRUCTURE OF EQUINE INFECTIOUS ANAEMIA VIRUS MATRIX ANTIGEN (EIAV MA)'''<br />
'''CRYSTAL STRUCTURE OF EQUINE INFECTIOUS ANAEMIA VIRUS MATRIX ANTIGEN (EIAV MA)'''<br />
==Overview==
==Overview==
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The Gag polyprotein is key to the budding of retroviruses from host cells, and is cleaved upon virion maturation, the N-terminal membrane-binding, domain forming the matrix protein (MA). The 2.8-A resolution crystal, structure of MA of equine infectious anemia virus (EIAV), a lentivirus, reveals that, despite showing no sequence similarity, more than half of, the molecule can be superimposed on the MAs of human immunodeficiency, virus type 1 (HIV-1) and simian immunodeficiency virus (SIV). However, unlike the structures formed by HIV-1 and SIV MAs, the oligomerization, state observed is not trimeric. We discuss the potential of this molecule, for membrane binding in the light of conformational differences between, EIAV MA and HIV or SIV MA.
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The Gag polyprotein is key to the budding of retroviruses from host cells and is cleaved upon virion maturation, the N-terminal membrane-binding domain forming the matrix protein (MA). The 2.8-A resolution crystal structure of MA of equine infectious anemia virus (EIAV), a lentivirus, reveals that, despite showing no sequence similarity, more than half of the molecule can be superimposed on the MAs of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV). However, unlike the structures formed by HIV-1 and SIV MAs, the oligomerization state observed is not trimeric. We discuss the potential of this molecule for membrane binding in the light of conformational differences between EIAV MA and HIV or SIV MA.
==About this Structure==
==About this Structure==
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1HEK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HEK OCA].
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1HEK is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Equine_infectious_anemia_virus Equine infectious anemia virus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HEK OCA].
==Reference==
==Reference==
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[[Category: Kingsman, A.]]
[[Category: Kingsman, A.]]
[[Category: Rao, Z.]]
[[Category: Rao, Z.]]
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[[Category: Stuart, D.I.]]
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[[Category: Stuart, D I.]]
[[Category: membrane-binding switching]]
[[Category: membrane-binding switching]]
[[Category: viral protein]]
[[Category: viral protein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:32:48 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:00:29 2008''

Revision as of 11:00, 21 February 2008


1hek, resolution 2.80Å

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CRYSTAL STRUCTURE OF EQUINE INFECTIOUS ANAEMIA VIRUS MATRIX ANTIGEN (EIAV MA)

Overview

The Gag polyprotein is key to the budding of retroviruses from host cells and is cleaved upon virion maturation, the N-terminal membrane-binding domain forming the matrix protein (MA). The 2.8-A resolution crystal structure of MA of equine infectious anemia virus (EIAV), a lentivirus, reveals that, despite showing no sequence similarity, more than half of the molecule can be superimposed on the MAs of human immunodeficiency virus type 1 (HIV-1) and simian immunodeficiency virus (SIV). However, unlike the structures formed by HIV-1 and SIV MAs, the oligomerization state observed is not trimeric. We discuss the potential of this molecule for membrane binding in the light of conformational differences between EIAV MA and HIV or SIV MA.

About this Structure

1HEK is a Single protein structure of sequence from Equine infectious anemia virus. Full crystallographic information is available from OCA.

Reference

Structure of equine infectious anemia virus matrix protein., Hatanaka H, Iourin O, Rao Z, Fry E, Kingsman A, Stuart DI, J Virol. 2002 Feb;76(4):1876-83. PMID:11799182

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