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PDBsum entry 3mjh
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Protein transport
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PDB id
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3mjh
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References listed in PDB file
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Key reference
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Title
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Structural basis for rab gtpase recognition and endosome tethering by the c2h2 zinc finger of early endosomal autoantigen 1 (eea1).
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Authors
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A.Mishra,
S.Eathiraj,
S.Corvera,
D.G.Lambright.
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Ref.
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Proc Natl Acad Sci U S A, 2010,
107,
10866-10871.
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PubMed id
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Note: In the PDB file this reference is
annotated as "TO BE PUBLISHED". The citation details given above have
been manually determined.
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Abstract
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Regulation of endosomal trafficking by Rab GTPases depends on selective
interactions with multivalent effectors, including EEA1 and Rabenosyn-5, which
facilitate endosome tethering, sorting, and fusion. Both EEA1 and Rabenosyn-5
contain a distinctive N-terminal C(2)H(2) zinc finger that binds Rab5. How these
C(2)H(2) zinc fingers recognize Rab GTPases remains unknown. Here, we report the
crystal structure of Rab5A in complex with the EEA1 C(2)H(2) zinc finger. The
binding interface involves all elements of the zinc finger as well as a short
N-terminal extension but is restricted to the switch and interswitch regions of
Rab5. High selectivity for Rab5 and, to a lesser extent Rab22, is observed in
quantitative profiles of binding to Rab family GTPases. Although critical
determinants are identified in both switch regions, Rab4-to-Rab5
conversion-of-specificity mutants reveal an essential requirement for additional
substitutions in the proximal protein core that are predicted to indirectly
influence recognition through affects on the structure and conformational
stability of the switch regions.
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