i want to khow whether glycophorin A in human red blood cell membrane is a single alpha helics trans membrane or a dimer one.
1AFO structure code is a dimer helix, so what happen to single helix?
please help me
thanks in advanced
Dear Fatemeh,
Glycophorin A transmembrane domain is a dimer.
The glycophorin A transmembrane domain dimer: Sequence-specific propensity for a right-handed supercoil of helixes
Herbert R. Treutlein, Mark A. Lemmon, Donald M. Engelman, Axel Brunger
Biochemistry, 1992, 31 (51), pp 12726–12732
DOI: 10.1021/bi00166a003
Publication Date: December 1992
http://pubs.acs.org/doi/abs/10.1021/bi00166a003
Biochemistry 1994, 33, 5539-5544 5539
Glycophorin A Helical Transmembrane Domains Dimerize in Phospholipid
Bilayers: A Resonance Energy Transfer Study7
Brian D. Adair and Donald M. Engelman'
Department of Molecular Biophysics and Biochemistry, Yale University, New Haven, Connecticut 06520
Received August 20, 1993; Revised Manuscript Received February 28, 1994"
For more information, see attached file.
Single helix protein:
Proteins. 2009 Mar;74(4):905-16. doi: 10.1002/prot.22183.
Charged single alpha-helix: a versatile protein structural motif.
Süveges D1, Gáspári Z, Tóth G, Nyitray L.
Author information
Abstract
A few highly charged natural peptide sequences were recently suggested to form stable alpha-helical structures in water. In this article we show that these sequences represent a novel structural motif called "charged single alpha-helix" (CSAH). To obtain reliable candidate CSAH motifs, we developed two conceptually different computational methods capable of scanning large databases: SCAN4CSAH is based on sequence features characteristic for salt bridge stabilized single alpha-helices, whereas FT_CHARGE applies Fourier transformation to charges along sequences. Using the consensus of the two approaches, a remarkable number of proteins were found to contain putative CSAH domains. Recombinant fragments (50-60 residues) corresponding to selected hits obtained by both methods (myosin 6, Golgi resident protein GCP60, and M4K4 protein kinase) were produced and shown by circular dichroism spectroscopy to adopt largely alpha-helical structure in water. CSAH segments differ substantially both from coiled-coil and intrinsically disordered proteins, despite the fact that current prediction methods recognize them as either or both. Analysis of the proteins containing CSAH motif revealed possible functional roles of the corresponding segments. The suggested main functional features include the formation of relatively rigid spacer/connector segments between functional domains as in caldesmon, extension of the lever arm in myosin motors and mediation of transient interactions by promoting dimerization in a range of proteins.
http://www.ncbi.nlm.nih.gov/pubmed/18712826
For simulation studies on this protein and others, see attached file.
Hoping this will be helpful,
Rafik
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