FIGURE

Fig. 3

ID

ZDB-FIG-250428-143

Publication

Yong et al., 2025 - Cryo-EM structure of the BLOC-3 complex provides insights into the pathogenesis of Hermansky-Pudlak syndrome

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Fig. 3

Comparative structural analysis reveals divergent assembly mechanisms of the BLOC-3 complex and other TLD RabGEFs.a, b Close-up views of the HPS1-HPS4 heterodimer interface illustrating electrostatic surface potential and conserved amino-acid residues (blue color represents conserved residues, while white color denotes non-conserved residues). c–e Detailed interactions of the interfaces between HPS1 (purple) and HPS4 (pink). Secondary structures of HPS1 and HPS4 are labeled as indicated. Residues critical for stabilizing the interface are shown in sticks. Black dashed lines indicate hydrogen bonds or salt bridges. Residues that are mutated in (f) are indicated with a yellow box. (f) HEK293T cells were transfected with Flag-tagged HPS4 and GFP-tagged HPS1 WT, L588P, L588A, R591E/Y592A(RY), K622E/Q624A(KQ), or D678R/V681A(DV) mutants, and subjected to GFP-nanotrap for immunoprecipitation. HPS1 and HPS4 were detected via antibodies against GFP and Flag, respectively. g Quantification of the results presented in (f). Statistical difference was determined by One-way ANOVA. Error bars represent the standard deviation of three independent biological repeats. n = 3. h HEK293T cells were transfected with GFP-tagged HPS1 and Flag-tagged HPS4 WT, 675-686GS or Δ675-686 mutant, and subjected to GFP-nanotrap for immunoprecipitation. HPS1 and HPS4 were detected via antibodies against GFP and Flag, respectively. (i) Quantification of the results presented in (h). Statistical difference was determined by One-way ANOVA. Error bars represent the standard deviation of three independent biological repeats. n = 3.

Expression Data

Expression Detail

Antibody Labeling

Phenotype Data

Phenotype Detail

Acknowledgments

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