TY  - JOUR
AU  - Stangler, T.
AU  - Tran, T.
AU  - Hoffmann, S.
AU  - Schmidt, H.
AU  - Jonas, E.
AU  - Willbold, D.
TI  - Competitive displacement of full-length HIV-1 Nef from the Hck SH3 domain by a high-affinity artificial peptide
JO  - Biological chemistry
VL  - 388
SN  - 1431-6730
CY  - Berlin [u.a.]
PB  - de Gruyter
M1  - PreJuSER-59381
SP  - 611 - 615
PY  - 2007
N1  - Record converted from VDB: 12.11.2012
AB  - 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.
KW  - Binding, Competitive
KW  - Gene Products, nef: metabolism
KW  - Humans
KW  - Peptides: metabolism
KW  - Protein Binding
KW  - Proto-Oncogene Proteins c-hck: metabolism
KW  - nef Gene Products, Human Immunodeficiency Virus
KW  - src Homology Domains
KW  - Gene Products, nef (NLM Chemicals)
KW  - Peptides (NLM Chemicals)
KW  - nef Gene Products, Human Immunodeficiency Virus (NLM Chemicals)
KW  - HCK protein, human (NLM Chemicals)
KW  - Proto-Oncogene Proteins c-hck (NLM Chemicals)
KW  - J (WoSType)
LB  - PUB:(DE-HGF)16
C6  - pmid:17552908
UR  - <Go to ISI:>//WOS:000247141500007
DO  - DOI:10.1515/BC.2007.075
UR  - https://juser.fz-juelich.de/record/59381
ER  -