3D Location of Conserved Motifs
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Superimposition of PTP domains 

X-ray crystal structures of vertebrate PTP domains show conserved fold and consistent Cα-backbone trace.

Alignment and superimposition of PTP1B (magenta), RPTPα (gray), RPTPμ (red), LAR (blue), SHP1 (green) and SHP2 (yellow)

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PyMol session files for interactive viewing of structures - pse | zip

3D location of conserved motifs in PTPs 

Core structures within the PTP domain are highly conserved (blue) and surface loops between secondary structure elements are least conserved (red)

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Proposed role of conserved residues in vertebrate PTP domains

Conserved motifs identified from our multiple sequence alignment of 113 vertebrate PTP domains (D2 sequences were not used in these evaluations; Andersen et al. MCB 2001).

Motifs are numbered (M1 - M10) in order of appearance in the primary amino acid sequence alignment. Amino acid numbering refer to to human PTP1B.
 

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Architecture of the PTP active site (Quick Time Movie)

Detailed view of key residues and structural elements involved in PTP substrate recognition. Shown is the active site of PTP1B in complex with a hexapeptide modeled on the EGF receptor. 

Click here to download this figure as a Quick Time movie file (13 MB). Get free QuickTime player here.

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