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Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein

Geyer, M. and Munte, C. E. and Schorr, J. and Kellner, R. and Kalbitzer, Hans Robert (1999) Structure of the anchor-domain of myristoylated and non-myristoylated HIV-1 Nef protein. Journal of molecular biology 289 (1), pp. 123-138.

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Abstract

Negative factor (Nef) is a regulatory myristoylated protein of human immunodeficiency virus (HIV) that has a two-domain structure consisting of an anchor domain and a core domain separated by a specific cleavage site of the HIV proteases. For structural analysis, the HIV-1 Nef anchor domain (residues 2-57) was synthesized with a myristoylated and non-myristoylated N terminus. The structures of ...

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Item Type:Article
Date:1999
Institutions:Biology, Preclinical Medicine > Institut für Biophysik und physikalische Biochemie > Prof. Dr. Dr. Hans Robert Kalbitzer
Identification Number:
ValueType
10339411PubMed ID
10.1006/jmbi.1999.2740DOI
Classification:
NotationType
Amino Acid SequenceMESH
Computer GraphicsMESH
Conserved SequenceMESH
Gene Products, nef/metabolismMESH
HIV-1MESH
HumansMESH
Models, MolecularMESH
Molecular Sequence DataMESH
Myristic Acid/metabolismMESH
Nuclear Magnetic Resonance, BiomolecularMESH
Peptide Fragments/chemistryMESH
Protein ConformationMESH
Protein Structure, SecondaryMESH
Sequence AlignmentMESH
SolubilityMESH
nef Gene Products, Human Immunodeficiency VirusMESH
Subjects:500 Science > 570 Life sciences
Status:Unknown
Refereed:Unknown
Created at the University of Regensburg:Yes
Owner: Gertraud Kellers
Deposited On:13 Sep 2010 08:05
Last Modified:13 Sep 2010 08:05
Item ID:16559
Owner Only: item control page
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