%0 Journal Article
%A Stangler, T.
%A Tran, T.
%A Hoffmann, S.
%A Schmidt, H.
%A Jonas, E.
%A Willbold, D.
%T Competitive displacement of full-length HIV-1 Nef from the Hck SH3 domain by a high-affinity artificial peptide
%J Biological chemistry
%V 388
%@ 1431-6730
%C Berlin [u.a.]
%I de Gruyter
%M PreJuSER-59381
%P 611 - 615
%D 2007
%Z Record converted from VDB: 12.11.2012
%X We studied the interaction of the artificial 12-aa proline-rich peptide PD1 with the SH3 domain of the hematopoietic cell kinase Hck and the peptide's potency in competitively displacing HIV-1 Nef from the Hck SH3 domain. PD1 was obtained from a phage display screen and exhibits exceptional affinity for the Hck SH3 domain (K(d)=0.23 microM). Competition experiments using NMR spectroscopy demonstrate that the peptide even displaces Nef from Hck SH3 and allow for estimation of the Nef-Hck SH3 dissociation constant (K(d)=0.44 microM), the strongest SH3 ligand interaction known so far. Consequences of this study for novel antiviral concepts are discussed.
%K Binding, Competitive
%K Gene Products, nef: metabolism
%K Humans
%K Peptides: metabolism
%K Protein Binding
%K Proto-Oncogene Proteins c-hck: metabolism
%K nef Gene Products, Human Immunodeficiency Virus
%K src Homology Domains
%K Gene Products, nef (NLM Chemicals)
%K Peptides (NLM Chemicals)
%K nef Gene Products, Human Immunodeficiency Virus (NLM Chemicals)
%K HCK protein, human (NLM Chemicals)
%K Proto-Oncogene Proteins c-hck (NLM Chemicals)
%K J (WoSType)
%F PUB:(DE-HGF)16
%9 Journal Article
%$ pmid:17552908
%U <Go to ISI:>//WOS:000247141500007
%R 10.1515/BC.2007.075
%U https://juser.fz-juelich.de/record/59381