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Journal article

Biophysical characterization of Vpu from HIV-1 suggests a channel-pore dualism.

Abstract:

Vpu from HIV-1 is an 81 amino acid type I integral membrane protein which consists of a cytoplasmic and a transmembrane (TM) domain. The TM domain is known to alter membrane permeability for ions and substrates when inserted into artificial membranes. Peptides corresponding to the TM domain of Vpu (Vpu(1-32)) and mutant peptides (Vpu(1-32)-W23L, Vpu(1-32)-R31V, Vpu(1-32)-S24L) have been synthesized and reconstituted into artificial lipid bilayers. All peptides show channel activity with a mai...

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Publication status:
Published

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Publisher copy:
10.1002/prot.21642

Authors


Mehnert, T More by this author
Fischer, D More by this author
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Journal:
Proteins
Volume:
70
Issue:
4
Pages:
1488-1497
Publication date:
2008-03-05
DOI:
EISSN:
1097-0134
ISSN:
0887-3585
URN:
uuid:64856273-36eb-436f-a741-e8f346d9842b
Source identifiers:
100053
Local pid:
pubs:100053

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