ATP7B Transmembrane Segments
 
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Metal-binding sites
  • MBS 1 [PDB]
  • MBS 2 [PDB]
  • MBS 3 [PDB]
  • MBS 4 [PDB]
  • MBS 5 [PDB]
  • MBS 6 [PDB]
  • Transmembrane Segments
  • TM Segment 1
  • TM Segment 2
  • TM Segment 3
  • TM Segment 4
  • TM Segment 5
  • TM Segment 6
  • TM Segment 7
  • TM Segment 8
  • ATP-Binding Domain
  • ATP BD structure model
  • Alignments
  • Cu-transporters
  • Phylogenetic tree [RESTRICTED]
  • WNDP mutations
     

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    Each page for the eight TMS shows results of the following analyses:

    • The positions of the transmembrane segments (TMS) were predicted with GCG Wisconsin Package’s TransMem program for human, mouse, rat, and sheep WNDP. Predicted TMS for each sequence are shaded in blue.
    • The boundaries of WNDP TMS were proposed based on the comparison of the predicted TMS in the alignment and are recorded on the top of the TMS pages.
    • Helical wheels were produced for each predicted TMS with WinPep. In each helical wheel, the labels of polar residues are in blue, while other residues are labeled in black.

    Polarity summary:
    TM segments 2,3,5,6, and 8 have more than three polar residues, and TM segments 1,4,7 have three or fewer polar residues.
    TM segments 1,2,4,7, and 8 have polar residues clustered on one side.
    TM segment 3,5,6 have polar residues across all sides.

    Invariantly conserved residues summary:
    There are no residues that are invariantly conserved residues across copper transporters in TM segments 1, and 5.
    There are three or fewer invariantly conserved residues in TM segments 2, 3, 4, 6, and 8.
    There are many invariantly conserved residues in TM segment 7.

    WNDP mutations summary:
    There are identified mutations in all TM segments.
    There are two or fewer WNDP mutation sites in TM segments 1, 3, 4, and 7.
    There are more than four WNDP mutation sites in TM segments 2, 5, 6, and 8.

     

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    Designed and maintained by Tina D. Purnat (purnatt@ohsu.edu).
    Last update: July 25, 2004.

    The Lutsenko Laboratory, Department of Biochemistry and Molecular Biology, MRB 624, Mail Code L224,
    Oregon Health & Science University, 3181 SW Sam Jackson Pk Rd, Portland, OR 97239-3098
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    This material is based upon work supported by the National Science Foundation
    under grant number MCB-0110057. Any opinions, findings, and conclusions or recommendations
    expressed in this material are those of the author(s) and do not necessarily reflect the views of the National Science Foundation.