Literature DB >> 11725124

Solution Structure of the Human CD4 (403-419) Receptor Peptide.

D. Willbold1, P. Rösch.   

Abstract

The cytoplasmic part of CD4 is known to be essential for the interaction with the human immunodeficiency virus type 1 proteins Vpu and Nef. The 17 amino acid synthetic peptide CD4 (403-419) with the amino acid sequence of the membrane proximal part of the cytoplasmic domain of the human CD4 receptor was structurally investigated by circular dichroism and nuclear magnetic resonance spectroscopy. The average alpha-helical content of the peptide could be estimated to be around 25%. Chemical shift index analysis and the connectivity pattern in nuclear Overhauser enhancement spectra located the alpha-helical part of the peptide from Gln403 to Arg412. It may be speculated that this amphipathic alpha-helix is the contact region with the Vpu and Nef proteins. Copyright 1996 S. Karger AG, Basel

Entities:  

Year:  1996        PMID: 11725124     DOI: 10.1007/bf02258047

Source DB:  PubMed          Journal:  J Biomed Sci        ISSN: 1021-7770            Impact factor:   8.410


  3 in total

1.  Direct in vitro binding of full-length human immunodeficiency virus type 1 Nef protein to CD4 cytoplasmic domain.

Authors:  A Preusser; L Briese; A S Baur; D Willbold
Journal:  J Virol       Date:  2001-04       Impact factor: 5.103

2.  Cluster of differentiation antigen 4 (CD4) endocytosis and adaptor complex binding require activation of the CD4 endocytosis signal by serine phosphorylation.

Authors:  C Pitcher; S Höning; A Fingerhut; K Bowers; M Marsh
Journal:  Mol Biol Cell       Date:  1999-03       Impact factor: 4.138

3.  Enhancing and inhibitory motifs regulate CD4 activity.

Authors:  Mark S Lee; Peter J Tuohy; Caleb Y Kim; Katrina Lichauco; Heather L Parrish; Koenraad Van Doorslaer; Michael S Kuhns
Journal:  Elife       Date:  2022-07-21       Impact factor: 8.713

  3 in total

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