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PDBsum entry 1elk
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Endocytosis/exocytosis
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PDB id
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1elk
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Structure of the vhs domain of human tom1 (target of myb 1): insights into interactions with proteins and membranes.
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Authors
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S.Misra,
B.M.Beach,
J.H.Hurley.
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Ref.
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Biochemistry, 2000,
39,
11282-11290.
[DOI no: ]
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PubMed id
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Abstract
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VHS domains are found at the N-termini of select proteins involved in
intracellular membrane trafficking. We have determined the crystal structure of
the VHS domain of the human Tom1 (target of myb 1) protein to 1.5 A resolution.
The domain consists of eight helices arranged in a superhelix. The surface of
the domain has two main features: (1) a basic patch on one side due to several
conserved positively charged residues on helix 3 and (2) a negatively charged
ridge on the opposite side, formed by residues on helix 2. We compare our
structure to the recently obtained structure of tandem VHS-FYVE domains from Hrs
[Mao, Y., Nickitenko, A., Duan, X., Lloyd, T. E., Wu, M. N., Bellen, H., and
Quiocho, F. A. (2000) Cell 100, 447-456]. Key features of the interaction
surface between the FYVE and VHS domains of Hrs, involving helices 2 and 4 of
the VHS domain, are conserved in the VHS domain of Tom1, even though Tom1 does
not have a FYVE domain. We also compare the structures of the VHS domains of
Tom1 and Hrs to the recently obtained structure of the ENTH domain of epsin-1
[Hyman, J., Chen, H., Di Fiore, P. P., De Camilli, P., and Brünger, A. T.
(2000) J. Cell Biol. 149, 537-546]. Comparison of the two VHS domains and the
ENTH domain reveals a conserved surface, composed of helices 2 and 4, that is
utilized for protein-protein interactions. In addition, VHS domain-containing
proteins are often localized to membranes. We suggest that the conserved
positively charged surface of helix 3 in VHS and ENTH domains plays a role in
membrane binding.
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Secondary reference #1
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Title
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Vhs domain marks a group of proteins involved in endocytosis and vesicular trafficking.
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Authors
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O.Lohi,
V.P.Lehto.
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Ref.
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Febs Lett, 1998,
440,
255-257.
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PubMed id
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