1hhv: Difference between revisions

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[[Image:1hhv.gif|left|200px]]<br /><applet load="1hhv" size="~~450~~" color="white" frame="true" align="right" spinBox="true"

[[Image:1hhv.gif|left|200px]]<br /><applet load="1hhv" size="350" color="white" frame="true" align="right" spinBox="true"

caption="1hhv" />

'''SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II'''<br />

==Overview==

Human herpesvirus-8 (HHV-8) is the infectious agent responsible for, Kaposi's sarcoma and encodes a protein, macrophage inflammatory protein-II, (vMIP-II), which shows sequence similarity to the human CC chemokines., vMIP-II has broad receptor specificity that crosses chemokine receptor, subfamilies, and inhibits HIV-1 viral entry mediated by numerous chemokine, receptors. In this study, the solution structure of chemically synthesized, vMIP-II was determined by nuclear magnetic resonance. The protein is a, monomer and possesses the chemokine fold consisting of a flexible, N-terminus, three antiparallel beta strands, and a C-terminal alpha helix., Except for the N-terminal residues (residues 1-13) and the last two, C-terminal residues (residues 73-74), the structure of vMIP-II is, well-defined, exhibiting average rmsd of 0.35 and 0.90 A for the backbone, heavy atoms and all heavy atoms of residues 14-72, respectively. Taking, into account the sequence differences between the various CC chemokines, and comparing their three-dimensional structures allows us to implicate, residues that influence the quaternary structure and receptor binding and, activation of these proteins in solution. The analysis of the sequence and, three-dimensional structure of vMIP-II indicates the presence of epitopes, involved in binding two receptors CCR2 and CCR5. We propose that vMIP-II, was initially specific for CCR5 and acquired receptor-binding properties, to CCR2 and other chemokine receptors.

Human herpesvirus-8 (HHV-8) is the infectious agent responsible for Kaposi's sarcoma and encodes a protein, macrophage inflammatory protein-II (vMIP-II), which shows sequence similarity to the human CC chemokines. vMIP-II has broad receptor specificity that crosses chemokine receptor subfamilies, and inhibits HIV-1 viral entry mediated by numerous chemokine receptors. In this study, the solution structure of chemically synthesized vMIP-II was determined by nuclear magnetic resonance. The protein is a monomer and possesses the chemokine fold consisting of a flexible N-terminus, three antiparallel beta strands, and a C-terminal alpha helix. Except for the N-terminal residues (residues 1-13) and the last two C-terminal residues (residues 73-74), the structure of vMIP-II is well-defined, exhibiting average rmsd of 0.35 and 0.90 A for the backbone heavy atoms and all heavy atoms of residues 14-72, respectively. Taking into account the sequence differences between the various CC chemokines and comparing their three-dimensional structures allows us to implicate residues that influence the quaternary structure and receptor binding and activation of these proteins in solution. The analysis of the sequence and three-dimensional structure of vMIP-II indicates the presence of epitopes involved in binding two receptors CCR2 and CCR5. We propose that vMIP-II was initially specific for CCR5 and acquired receptor-binding properties to CCR2 and other chemokine receptors.

==About this Structure==

1HHV 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://~~ispc~~.weizmann.ac.il/oca-bin/ocashort?id=1HHV OCA].

1HHV 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=1HHV OCA].

==Reference==

Line 14:

[[Category: Fernandez, E.]]

[[Category: Lolis, E.]]

[[Category: Navenot, J.M.]]

[[Category: Navenot, J M.]]

[[Category: Pepiper, S.]]

[[Category: Schweitzer, B.I.]]

[[Category: Schweitzer, B I.]]

[[Category: Shao, W.]]

[[Category: Thompson, D.A.]]

[[Category: Thompson, D A.]]

[[Category: Wilken, J.]]

[[Category: kshv(human herpesvirus 8)]]

Line 26:

[[Category: vmip-ii]]

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@@ Line 1: / Line 1: @@
-[[Image:1hhv.gif|left|200px]]<br /><applet load="1hhv" size="450" color="white" frame="true" align="right" spinBox="true"
+[[Image:1hhv.gif|left|200px]]<br /><applet load="1hhv" size="350" color="white" frame="true" align="right" spinBox="true"
 caption="1hhv" />
 '''SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II'''<br />
 ==Overview==
-Human herpesvirus-8 (HHV-8) is the infectious agent responsible for, Kaposi's sarcoma and encodes a protein, macrophage inflammatory protein-II, (vMIP-II), which shows sequence similarity to the human CC chemokines., vMIP-II has broad receptor specificity that crosses chemokine receptor, subfamilies, and inhibits HIV-1 viral entry mediated by numerous chemokine, receptors. In this study, the solution structure of chemically synthesized, vMIP-II was determined by nuclear magnetic resonance. The protein is a, monomer and possesses the chemokine fold consisting of a flexible, N-terminus, three antiparallel beta strands, and a C-terminal alpha helix., Except for the N-terminal residues (residues 1-13) and the last two, C-terminal residues (residues 73-74), the structure of vMIP-II is, well-defined, exhibiting average rmsd of 0.35 and 0.90 A for the backbone, heavy atoms and all heavy atoms of residues 14-72, respectively. Taking, into account the sequence differences between the various CC chemokines, and comparing their three-dimensional structures allows us to implicate, residues that influence the quaternary structure and receptor binding and, activation of these proteins in solution. The analysis of the sequence and, three-dimensional structure of vMIP-II indicates the presence of epitopes, involved in binding two receptors CCR2 and CCR5. We propose that vMIP-II, was initially specific for CCR5 and acquired receptor-binding properties, to CCR2 and other chemokine receptors.
+Human herpesvirus-8 (HHV-8) is the infectious agent responsible for Kaposi's sarcoma and encodes a protein, macrophage inflammatory protein-II (vMIP-II), which shows sequence similarity to the human CC chemokines. vMIP-II has broad receptor specificity that crosses chemokine receptor subfamilies, and inhibits HIV-1 viral entry mediated by numerous chemokine receptors. In this study, the solution structure of chemically synthesized vMIP-II was determined by nuclear magnetic resonance. The protein is a monomer and possesses the chemokine fold consisting of a flexible N-terminus, three antiparallel beta strands, and a C-terminal alpha helix. Except for the N-terminal residues (residues 1-13) and the last two C-terminal residues (residues 73-74), the structure of vMIP-II is well-defined, exhibiting average rmsd of 0.35 and 0.90 A for the backbone heavy atoms and all heavy atoms of residues 14-72, respectively. Taking into account the sequence differences between the various CC chemokines and comparing their three-dimensional structures allows us to implicate residues that influence the quaternary structure and receptor binding and activation of these proteins in solution. The analysis of the sequence and three-dimensional structure of vMIP-II indicates the presence of epitopes involved in binding two receptors CCR2 and CCR5. We propose that vMIP-II was initially specific for CCR5 and acquired receptor-binding properties to CCR2 and other chemokine receptors.
 ==About this Structure==
-HHV 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://ispc.weizmann.ac.il/oca-bin/ocashort?id=1HHV OCA].
+HHV 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=1HHV OCA].
 ==Reference==
@@ Line 14: / Line 14: @@
 [[Category: Fernandez, E.]]
 [[Category: Lolis, E.]]
-[[Category: Navenot, J.M.]]
+[[Category: Navenot, J M.]]
 [[Category: Pepiper, S.]]
-[[Category: Schweitzer, B.I.]]
+[[Category: Schweitzer, B I.]]
 [[Category: Shao, W.]]
-[[Category: Thompson, D.A.]]
+[[Category: Thompson, D A.]]
 [[Category: Wilken, J.]]
 [[Category: kshv(human herpesvirus 8)]]
@@ Line 26: / Line 26: @@
 [[Category: vmip-ii]]
-''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 16:35:43 2007''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:01:23 2008''