1cm9: Difference between revisions

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[[Image:1cm9.png|left|200px]]
<!--
The line below this paragraph, containing "STRUCTURE_1cm9", creates the "Structure Box" on the page.
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{{STRUCTURE_1cm9|  PDB=1cm9  |  SCENE=  }}  
{{STRUCTURE_1cm9|  PDB=1cm9  |  SCENE=  }}  
===CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II===
===CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II===
{{ABSTRACT_PUBMED_11041848}}


 
==Function==
<!--
[[http://www.uniprot.org/uniprot/VMI2_HHV8 VMI2_HHV8]] Blocks infection by several different human immunodeficiency virus type 1 (HIV-1) strains. This occurs because vMIP-II binds to a wide range of chemokine receptors. May form part of the response to host defenses contributing to virus-induced neoplasia and may have relevance to KSHV and HIV-I interactions.
The line below this paragraph, {{ABSTRACT_PUBMED_11041848}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_11041848}}


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:011041848</ref><references group="xtra"/>
<ref group="xtra">PMID:011041848</ref><references group="xtra"/><references/>
[[Category: Human herpesvirus 8]]
[[Category: Human herpesvirus 8]]
[[Category: Fernandez, E J.]]
[[Category: Fernandez, E J.]]

Revision as of 06:32, 10 April 2014

Template:STRUCTURE 1cm9

CRYSTAL STRUCTURE OF VIRAL MACROPHAGE INFLAMMATORY PROTEIN-II

Template:ABSTRACT PUBMED 11041848

Function

[VMI2_HHV8] Blocks infection by several different human immunodeficiency virus type 1 (HIV-1) strains. This occurs because vMIP-II binds to a wide range of chemokine receptors. May form part of the response to host defenses contributing to virus-induced neoplasia and may have relevance to KSHV and HIV-I interactions.

About this Structure

1cm9 is a 2 chain structure with sequence from Human herpesvirus 8. Full crystallographic information is available from OCA.

Reference

  1. Fernandez EJ, Wilken J, Thompson DA, Peiper SC, Lolis E. Comparison of the structure of vMIP-II with eotaxin-1, RANTES, and MCP-3 suggests a unique mechanism for CCR3 activation. Biochemistry. 2000 Oct 24;39(42):12837-44. PMID:11041848

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