 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 1]](bw5397fig1mag.jpg)
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Figure 1
Schematic diagram of the RPTPγ sequence. The hydrophobic signal peptide (residues 1–19) and the transmembrane domain (residues 737–760) are indicated by filled rectangles. The extracellular portion of RPTPγ includes a carbonic anhydrase homology domain (CAH) and a fibronectin III homology domain (FN). The intracellular portion of RPTPγ includes a protein tyrosine phosphatase catalytic domain (D1) and a protein tyrosine phosphatase-like domain (D2) in which the catalytic cysteine is replaced by an aspartate. Domains D1 and D2 as shown in the diagram include the α1′ and α2′ helices as defined by Barford et al. (1994  ), since PTPμ (PDB entry 1rpm
) on which the construct design for PTPγ was based had sequences in these regions that were helical. |
![[Figure 1]](bw5397fig1.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
