1hhv: Difference between revisions
No edit summary |
No edit summary |
||
| Line 1: | Line 1: | ||
[[Image:1hhv.gif|left|200px]] | [[Image:1hhv.gif|left|200px]] | ||
<!-- | |||
The line below this paragraph, containing "STRUCTURE_1hhv", creates the "Structure Box" on the page. | |||
You may change the PDB parameter (which sets the PDB file loaded into the applet) | |||
or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |||
| | or leave the SCENE parameter empty for the default display. | ||
| | --> | ||
{{STRUCTURE_1hhv| PDB=1hhv | SCENE= }} | |||
}} | |||
'''SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II''' | '''SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II''' | ||
| Line 19: | Line 16: | ||
==About this Structure== | ==About this Structure== | ||
1HHV is a [[Single protein]] structure | 1HHV is a [[Single protein]] structure. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HHV OCA]. | ||
==Reference== | ==Reference== | ||
| Line 32: | Line 29: | ||
[[Category: Thompson, D A.]] | [[Category: Thompson, D A.]] | ||
[[Category: Wilken, J.]] | [[Category: Wilken, J.]] | ||
[[Category: | [[Category: Nmr structure]] | ||
[[Category: Receptor binding]] | |||
[[Category: | [[Category: Virus chemokine]] | ||
[[Category: | [[Category: Vmip-ii]] | ||
[[Category: | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 18:51:33 2008'' | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | |||
Revision as of 15:51, 2 May 2008
SOLUTION STRUCTURE OF VIRUS CHEMOKINE VMIP-II
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.
About this Structure
1HHV is a Single protein structure. Full crystallographic information is available from OCA.
Reference
CCR2 and CCR5 receptor-binding properties of herpesvirus-8 vMIP-II based on sequence analysis and its solution structure., Shao W, Fernandez E, Sachpatzidis A, Wilken J, Thompson DA, Schweitzer BI, Lolis E, Eur J Biochem. 2001 May;268(10):2948-59. PMID:11358512 Page seeded by OCA on Fri May 2 18:51:33 2008
