1elk

<table><tr><td colspan='2'>[[1elk]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ELK OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ELK FirstGlance]. <br>

</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1elk FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1elk OCA], [http://pdbe.org/1elk PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1elk RCSB], [http://www.ebi.ac.uk/pdbsum/1elk PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1elk ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/TOM1_HUMAN TOM1_HUMAN]] May be involved in intracellular trafficking. Probable association with membranes.

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== Publication Abstract from PubMed ==

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 Brunger, 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.

Structure of the VHS domain of human Tom1 (target of myb 1): insights into interactions with proteins and membranes.,Misra S, Beach BM, Hurley JH Biochemistry. 2000 Sep 19;39(37):11282-90. PMID:10985773<ref>PMID:10985773</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

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<div class="pdbe-citations 1elk" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Human]]

[[Category: Beach, B]]

[[Category: Hurley, J H]]

[[Category: Misra, S]]

[[Category: Superhelix of helice]]