1vmp
From Proteopedia
Line 7: | Line 7: | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
+ | |DOMAIN= | ||
+ | |RELATEDENTRY= | ||
+ | |RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1vmp FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1vmp OCA], [http://www.ebi.ac.uk/pdbsum/1vmp PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1vmp RCSB]</span> | ||
}} | }} | ||
Line 16: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
- | 1VMP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1VMP is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_8 Human herpesvirus 8]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1VMP OCA]. |
==Reference== | ==Reference== | ||
The solution structure of the anti-HIV chemokine vMIP-II., Liwang AC, Wang ZX, Sun Y, Peiper SC, Liwang PJ, Protein Sci. 1999 Nov;8(11):2270-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10595530 10595530] | The solution structure of the anti-HIV chemokine vMIP-II., Liwang AC, Wang ZX, Sun Y, Peiper SC, Liwang PJ, Protein Sci. 1999 Nov;8(11):2270-80. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10595530 10595530] | ||
- | [[Category: Human herpesvirus | + | [[Category: Human herpesvirus 8]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Liwang, A C.]] | [[Category: Liwang, A C.]] | ||
Line 35: | Line 38: | ||
[[Category: vmip-ii]] | [[Category: vmip-ii]] | ||
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Mar 31 00:26:32 2008'' |
Revision as of 21:26, 30 March 2008
| |||||||
Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
Coordinates: | save as pdb, mmCIF, xml |
STRUCTURE OF THE ANTI-HIV CHEMOKINE VMIP-II
Overview
We report the solution structure of the chemotactic cytokine (chemokine) vMIP-II. This protein has unique biological activities in that it 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, some of which are used by HJV to gain cell entry. vMIP-II is a monomeric protein, unlike most members of the chemokine family, and its structure consists of a disordered N-terminus, followed by a helical turn (Gln25-Leu27), which leads into the first strand of a three-stranded antiparallel beta-sheet (Ser29-Thr34; Gly42-Thr47; Gln52-Asp56). Following the sheet is a C-terminal alpha-helix, which extends from residue Asp60 until Gln68. The final five residues beyond the C-terminal helix (Pro70-Arg74) are in an extended conformation, but several of these C-terminal residues contact the first beta-strand. The structure of vMIP-II is compared to other chemokines that also block infection by HIV-1, and the structural basis of its lack of ability to form a dimer is discussed.
About this Structure
1VMP is a Single protein structure of sequence from Human herpesvirus 8. Full crystallographic information is available from OCA.
Reference
The solution structure of the anti-HIV chemokine vMIP-II., Liwang AC, Wang ZX, Sun Y, Peiper SC, Liwang PJ, Protein Sci. 1999 Nov;8(11):2270-80. PMID:10595530
Page seeded by OCA on Mon Mar 31 00:26:32 2008
Categories: Human herpesvirus 8 | Single protein | Liwang, A C. | Liwang, P J. | Peiper, S C. | Sun, Y. | Wang, Z X. | Chemokine | Herpesvirus | Hhv-8 | Kaposis' | Monomer | Sarcoma | Vmip-ii