1zec: Difference between revisions
No edit summary |
No edit summary |
||
| Line 4: | Line 4: | ||
|PDB= 1zec |SIZE=350|CAPTION= <scene name='initialview01'>1zec</scene> | |PDB= 1zec |SIZE=350|CAPTION= <scene name='initialview01'>1zec</scene> | ||
|SITE= | |SITE= | ||
|LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> | |LIGAND= <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene> | ||
|ACTIVITY= | |ACTIVITY= | ||
|GENE= N-TERMINAL FRAGMENT OF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1]) | |GENE= N-TERMINAL FRAGMENT OF ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=11676 Human immunodeficiency virus 1]) | ||
|DOMAIN= | |||
|RELATEDENTRY= | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1zec FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1zec OCA], [http://www.ebi.ac.uk/pdbsum/1zec PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1zec RCSB]</span> | |||
}} | }} | ||
| Line 27: | Line 30: | ||
[[Category: Monks, S A.]] | [[Category: Monks, S A.]] | ||
[[Category: Norton, R S.]] | [[Category: Norton, R S.]] | ||
[[Category: cytolysin]] | [[Category: cytolysin]] | ||
[[Category: polypeptide]] | [[Category: polypeptide]] | ||
[[Category: viral peptide]] | [[Category: viral peptide]] | ||
''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 01:34:46 2008'' | ||
Revision as of 01:34, 31 March 2008
| |||||||
| Ligands: | , | ||||||
| Gene: | N-TERMINAL FRAGMENT OF (Human immunodeficiency virus 1) | ||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
NMR SOLUTION STRUCTURE OF NEF1-25, 20 STRUCTURES
OverviewOverview
Nef is a 27 kDa myristylated phosphoprotein expressed early in infection by HIV. The N terminus of Nef is thought to play a vital role in the functions of this protein through its interactions with membrane structures. The solution structure of a 25-residue polypeptide corresponding to the N terminus of Nef (Nef1-25) has been investigated by 1H NMR spectroscopy. In aqueous solution at pH 4.8 and 281 K, this peptide underwent conformational averaging, with Pro13 existing in cis and trans conformations in nearly equal proportions. In methanol solution, however, the peptide adopted a well-defined alpha-helical structure from residues 6 to 22, with the N- and C-terminal regions having a less ordered structure. On the basis of a comparison of chemical shifts and NOEs, it appeared that this helical structure was maintained in aqueous trifluoroethanol (50% v/v) and to a lesser extent in a solution of SDS micelles. When the N-acetyl group was replaced by either an N-myristyl or a free ammonium group, there was little effect on the three-dimensional structure of the peptide in methanol; deamidation of the C terminus also had no effect on the structure in methanol. In water, the myristylated peptide aggregated. The similarity between the sequences of Nef1-25 and melittin is reflected in the similar structures of the two molecules, although the N-terminal helix of melittin is more defined. This similarity in structure raises the possibility that Nef1-25 not only interacts with membranes but also may be capable of disrupting them and causing cell lysis. This type of interaction could contribute at least in part to the killing of bystander cells in lymphoid tissues during HIV infection.
About this StructureAbout this Structure
1ZEC is a Single protein structure of sequence from Human immunodeficiency virus 1. Full crystallographic information is available from OCA.
ReferenceReference
Solution structure of a polypeptide from the N terminus of the HIV protein Nef., Barnham KJ, Monks SA, Hinds MG, Azad AA, Norton RS, Biochemistry. 1997 May 20;36(20):5970-80. PMID:9166767
Page seeded by OCA on Mon Mar 31 01:34:46 2008