1lcs

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(New page: 200px<br /><applet load="1lcs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1lcs, resolution 2.5&Aring;" /> '''RECEPTOR-BINDING DOMA...)
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caption="1lcs, resolution 2.5&Aring;" />
'''RECEPTOR-BINDING DOMAIN FROM SUBGROUP B FELINE LEUKEMIA VIRUS'''<br />
'''RECEPTOR-BINDING DOMAIN FROM SUBGROUP B FELINE LEUKEMIA VIRUS'''<br />
==Overview==
==Overview==
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Infection of T lymphocytes by the cytopathic retrovirus feline leukemia, virus subgroup T (FeLV-T) requires FeLIX, a cellular coreceptor that is, encoded by an endogenous provirus and closely resembles the, receptor-binding domain (RBD) of feline leukemia virus subgroup B, (FeLV-B). We determined the structure of FeLV-B RBD, which has FeLIX, activity, to a 2.5-A resolution by X-ray crystallography. The structure of, the receptor-specific subdomain of this glycoprotein differs dramatically, from that of Friend murine leukemia virus (Fr-MLV), which binds a, different cell surface receptor. Remarkably, we find that Fr-MLV RBD also, activates FeLV-T infection of cells expressing the Fr-MLV receptor and, that FeLV-B RBD is a competitive inhibitor of infection under these, conditions. These studies suggest that FeLV-T infection relies on the, following property of mammalian leukemia virus RBDs: the ability to couple, interaction with one of a variety of receptors to the activation of a, conserved membrane fusion mechanism. A comparison of the FeLV-B and Fr-MLV, RBD structures illustrates how receptor-specific regions are linked to, conserved elements critical for postbinding events in virus entry.
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Infection of T lymphocytes by the cytopathic retrovirus feline leukemia virus subgroup T (FeLV-T) requires FeLIX, a cellular coreceptor that is encoded by an endogenous provirus and closely resembles the receptor-binding domain (RBD) of feline leukemia virus subgroup B (FeLV-B). We determined the structure of FeLV-B RBD, which has FeLIX activity, to a 2.5-A resolution by X-ray crystallography. The structure of the receptor-specific subdomain of this glycoprotein differs dramatically from that of Friend murine leukemia virus (Fr-MLV), which binds a different cell surface receptor. Remarkably, we find that Fr-MLV RBD also activates FeLV-T infection of cells expressing the Fr-MLV receptor and that FeLV-B RBD is a competitive inhibitor of infection under these conditions. These studies suggest that FeLV-T infection relies on the following property of mammalian leukemia virus RBDs: the ability to couple interaction with one of a variety of receptors to the activation of a conserved membrane fusion mechanism. A comparison of the FeLV-B and Fr-MLV RBD structures illustrates how receptor-specific regions are linked to conserved elements critical for postbinding events in virus entry.
==About this Structure==
==About this Structure==
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1LCS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viruses Viruses] with TOE as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1LCS OCA].
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1LCS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Viruses Viruses] with <scene name='pdbligand=TOE:'>TOE</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LCS OCA].
==Reference==
==Reference==
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[[Category: Single protein]]
[[Category: Single protein]]
[[Category: Viruses]]
[[Category: Viruses]]
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[[Category: Barnett, A.L.]]
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[[Category: Barnett, A L.]]
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[[Category: Cunningham, J.M.]]
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[[Category: Cunningham, J M.]]
[[Category: Fass, D.]]
[[Category: Fass, D.]]
[[Category: Li, W.]]
[[Category: Li, W.]]
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[[Category: Wensel, D.L.]]
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[[Category: Wensel, D L.]]
[[Category: TOE]]
[[Category: TOE]]
[[Category: antiparallel beta-sandwich glycoprotein]]
[[Category: antiparallel beta-sandwich glycoprotein]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 20:28:57 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:43:46 2008''

Revision as of 11:43, 21 February 2008


1lcs, resolution 2.5Å

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RECEPTOR-BINDING DOMAIN FROM SUBGROUP B FELINE LEUKEMIA VIRUS

Overview

Infection of T lymphocytes by the cytopathic retrovirus feline leukemia virus subgroup T (FeLV-T) requires FeLIX, a cellular coreceptor that is encoded by an endogenous provirus and closely resembles the receptor-binding domain (RBD) of feline leukemia virus subgroup B (FeLV-B). We determined the structure of FeLV-B RBD, which has FeLIX activity, to a 2.5-A resolution by X-ray crystallography. The structure of the receptor-specific subdomain of this glycoprotein differs dramatically from that of Friend murine leukemia virus (Fr-MLV), which binds a different cell surface receptor. Remarkably, we find that Fr-MLV RBD also activates FeLV-T infection of cells expressing the Fr-MLV receptor and that FeLV-B RBD is a competitive inhibitor of infection under these conditions. These studies suggest that FeLV-T infection relies on the following property of mammalian leukemia virus RBDs: the ability to couple interaction with one of a variety of receptors to the activation of a conserved membrane fusion mechanism. A comparison of the FeLV-B and Fr-MLV RBD structures illustrates how receptor-specific regions are linked to conserved elements critical for postbinding events in virus entry.

About this Structure

1LCS is a Single protein structure of sequence from Viruses with as ligand. Full crystallographic information is available from OCA.

Reference

Structure and mechanism of a coreceptor for infection by a pathogenic feline retrovirus., Barnett AL, Wensel DL, Li W, Fass D, Cunningham JM, J Virol. 2003 Feb;77(4):2717-29. PMID:12552012

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