1qlo
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=1qlo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1qlo OCA], [http://www.ebi.ac.uk/pdbsum/1qlo PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1qlo RCSB]</span> | ||
}} | }} | ||
| Line 16: | Line 19: | ||
==About this Structure== | ==About this Structure== | ||
| - | 1QLO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/ | + | 1QLO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Human_herpesvirus_1 Human herpesvirus 1]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1QLO OCA]. |
==Reference== | ==Reference== | ||
Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy., Pfander R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampe R, Biochemistry. 1999 Oct 12;38(41):13692-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10521276 10521276] | Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy., Pfander R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampe R, Biochemistry. 1999 Oct 12;38(41):13692-8. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/10521276 10521276] | ||
| - | [[Category: Human herpesvirus | + | [[Category: Human herpesvirus 1]] |
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Holak, T A.]] | [[Category: Holak, T A.]] | ||
| Line 32: | Line 35: | ||
[[Category: protein icp47]] | [[Category: protein icp47]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 23:15:29 2008'' |
Revision as of 20:15, 30 March 2008
| |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
STRUCTURE OF THE ACTIVE DOMAIN OF THE HERPES SIMPLEX VIRUS PROTEIN ICP47 IN WATER/SODIUM DODECYL SULFATE SOLUTION DETERMINED BY NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY
Overview
ICP47 encoded by herpes simplex virus (HSV) is a key factor in the evasion of cellular immune response against HSV-infected cells. By specific inhibition of the transporter associated with antigen processing (TAP), ICP47 prevents peptide transport into the endoplasmic reticulum and subsequent loading of major histocompatibility complex (MHC) class I molecules. Amino acid residues 3-34 have been identified as the active domain. This domain appeared to be unstructured in aqueous solution, whereas after binding to membranes an alpha-helical conformation was observed. Here, we have analyzed the structure of ICP47(2-34) in a lipidlike environment by nuclear magnetic resonance (NMR) spectroscopy. In micellar solution of deuterated sodium dodecyl sulfate, the viral TAP inhibitor adopts an ordered structure. There are two helical regions extending from residues 4 to 15 and from residues 22 to 32. Arg-16 is found on the C-terminus of the first helix, and Gly-33 serves as a terminator of the second helix. A loop between residues 17 and 21 is also evident in the structure. The relative orientation of the helices toward each other, however, could not be determined due to the paucity of NOEs from residues 18-21.
About this Structure
1QLO is a Single protein structure of sequence from Human herpesvirus 1. Full crystallographic information is available from OCA.
Reference
Structure of the active domain of the herpes simplex virus protein ICP47 in water/sodium dodecyl sulfate solution determined by nuclear magnetic resonance spectroscopy., Pfander R, Neumann L, Zweckstetter M, Seger C, Holak TA, Tampe R, Biochemistry. 1999 Oct 12;38(41):13692-8. PMID:10521276
Page seeded by OCA on Sun Mar 30 23:15:29 2008
