 | Acta Crystallographica Section F Acta Crystallographica Section F STRUCTURAL BIOLOGY COMMUNICATIONS |
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![[Figure 2]](rs5005fig2mag.jpg)
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Figure 2
Conformational heterogeneity across the PTP1B allosteric network in an SSX RT structure. (a) Overview of the key sites in PTP1B featured in (b)–(d). (b) The active-site WPD loop is best modeled as adopting only the open conformation, based on 2Fo − Fc electron density contoured at 1σ (blue) and positive/negative Fo − Fc difference electron density contoured at ±3.0σ (green/red). The closed conformation of the WPD loop as modeled in PDB entry 1sug (transparent cyan) is shown for comparison. See also Supplementary Fig. S4 (dual conformation). (c) The α7 helix is best modeled as disordered, based on 2Fo − Fc density at 1σ and Fo − Fc density at ±3.0σ. The ordered conformation of α7 from PDB entry 1sug is shown for comparison. Note the absence of strong density for the Trp291 `anchor' that can occupy the allosteric BB site (arrow). See also Supplementary Fig. S5 (α7 refined). (d) In contrast to the WPD loop and α7, Loop 16 definitively adopts alternate conformations with similar occupancies, based on 2Fo − Fc density at 1σ and Fo − Fc density at ±3.0σ. See also Supplementary Fig. S5 (omit maps). |
![[Figure 2]](rs5005fig2.jpg)
| STRUCTURAL BIOLOGY COMMUNICATIONS |
ISSN: 2053-230X
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