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Details on Person In its inactive nucleotide-free state, guanylate-binding pro...

Class:IdSummation:9968552
_displayNameIn its inactive nucleotide-free state, guanylate-binding pro...
_timestamp2025-10-16 05:26:19
created[InstanceEdit:9968554] Shamovsky, Veronica, 2025-10-16
literatureReference[LiteratureReference:9947948] Human GBP1 binds LPS to initiate assembly of a caspase-4 activating platform on cytosolic bacteria
[LiteratureReference:9947834] Nucleotide-dependent farnesyl switch orchestrates polymerization and membrane binding of human guanylate-binding protein 1
[LiteratureReference:9947892] Structural basis of antimicrobial membrane coat assembly by human GBP1
[LiteratureReference:9947890] Structural insights into the activation mechanism of antimicrobial GBP1
[LiteratureReference:9947832] Structural requirements for membrane binding of human guanylate-binding protein 1
[LiteratureReference:9947914] Catalytic activity of human guanylate-binding protein 1 coupled to the release of structural restraints imposed by the C-terminal domain
[LiteratureReference:9947909] Direct binding of polymeric GBP1 to LPS disrupts bacterial cell envelope functions
textIn its inactive nucleotide-free state, guanylate-binding protein 1 (GBP1) exists as a monomer in which the C-terminal farnesyl group is sequestered within a hydrophobic pocket, preventing membrane association. Upon GTP binding, GBP1 undergoes conformational rearrangements that expose the farnesyl moiety, enabling membrane interaction, activation of its GTPase cycle, and oligomerization on lipopolysaccharide (LPS)-rich outer membranes of cytosolic Gram-negative bacteria (Shydlovskyi S et al., 2017; Kutsch M et al., 2020; Santos JC et al., 2020; Sistemich L et al., 2021; Ince S et al., 2021; Weismehl M et al., 2024; Kuhm T et al., 2025).
(summation)[Reaction:9968553] GBP1 binds GTP [Homo sapiens]
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