Competitive displacement of full-length HIV-1 Nef from the Hck SH3 domain by a high-affinity artificial peptide

Stangler, T.; Tran, T.; Willbold, D.; Schmidt, H.; Hoffmann, S.; Jonas, E.

doi:10.1515/BC.2007.075

Journal Article

Competitive displacement of full-length HIV-1 Nef from the Hck SH3 domain by a high-affinity artificial peptide

Stangler, T.FZJ* ; Tran, T.FZJ* ; Hoffmann, S.FZJ* ; Schmidt, H.FZJ* ; Jonas, E.FZJ* ; Willbold, D.FZJ*

2007
de Gruyter Berlin [u.a.]

Biological chemistry 388, 611 - 615 (2007) [10.1515/BC.2007.075]

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Please use a persistent id in citations: http://hdl.handle.net/2128/18399 doi:10.1515/BC.2007.075

Abstract: 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.

Keyword(s): Binding, Competitive (MeSH) ; Gene Products, nef: metabolism (MeSH) ; Humans (MeSH) ; Peptides: metabolism (MeSH) ; Protein Binding (MeSH) ; Proto-Oncogene Proteins c-hck: metabolism (MeSH) ; nef Gene Products, Human Immunodeficiency Virus (MeSH) ; src Homology Domains (MeSH) ; Gene Products, nef ; Peptides ; nef Gene Products, Human Immunodeficiency Virus ; HCK protein, human ; Proto-Oncogene Proteins c-hck ; J ; competition (auto) ; Hck (auto) ; HIV (auto) ; Nef (auto) ; NMR (auto) ; protein-peptide interaction (auto) ; SH3 (auto)