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PDBsum entry 5efx
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Signaling protein
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PDB id
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5efx
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References listed in PDB file
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Key reference
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Title
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Crystal structure of hgef-H1 ph domain provides insight into incapability in phosphoinositide binding.
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Authors
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Y.Jiang,
H.Jiang,
S.Zhou,
B.Meng,
Z.J.Liu,
S.Ouyang.
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Ref.
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Biochem Biophys Res Commun, 2016,
471,
621-627.
[DOI no: ]
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PubMed id
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Abstract
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The guanine nucleotide exchange factor GEF-H1 (also known as ARHGEF2) is
identified as a member of the Dbl family of GEFs. It regulates RhoA-dependent
cell signaling pathways and plays important roles in biological processes.
GEF-H1 contains an N-terminal zinc finger domain, a Dbl-homologous (DH) domain
followed by a Pleckstrin homology (PH) domain, and a C-terminal domain. The
specific roles of its PH domain are poorly understood. Here we report the
crystal structure of human GEF-H1 PH domain to 2.45 Å resolution. A conserved
surface is formed by β8, β9, β10, and it may mediate protein-protein
interactions. Although the folding resembles other PH domains that have defined
structures, superposition of different PH domains clearly shows that the loop
between β6/β7 and the loop between β3/β4 are so close that they will prevent
its binding with phosphoinositide due to steric hindrance, and this has been
proved by isothermal titration calorimetry (ITC) and thermal shift assay (TSA).
Our studies provide a structural framework for further work on the function of
GEF-H1.
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