1elk

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
[[Image:1elk.gif|left|200px]]
[[Image:1elk.gif|left|200px]]
-
{{Structure
+
<!--
-
|PDB= 1elk |SIZE=350|CAPTION= <scene name='initialview01'>1elk</scene>, resolution 1.5&Aring;
+
The line below this paragraph, containing "STRUCTURE_1elk", creates the "Structure Box" on the page.
-
|SITE=
+
You may change the PDB parameter (which sets the PDB file loaded into the applet)
-
|LIGAND=
+
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-
|ACTIVITY=
+
or leave the SCENE parameter empty for the default display.
-
|GENE=
+
-->
-
|DOMAIN=
+
{{STRUCTURE_1elk| PDB=1elk | SCENE= }}
-
|RELATEDENTRY=
+
-
|RESOURCES=<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://www.ebi.ac.uk/pdbsum/1elk PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1elk RCSB]</span>
+
-
}}
+
'''VHS domain of TOM1 protein from H. sapiens'''
'''VHS domain of TOM1 protein from H. sapiens'''
Line 28: Line 25:
[[Category: Hurley, J H.]]
[[Category: Hurley, J H.]]
[[Category: Misra, S.]]
[[Category: Misra, S.]]
-
[[Category: superhelix of helice]]
+
[[Category: Superhelix of helice]]
-
 
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 15:14:56 2008''
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 20:05:00 2008''
+

Revision as of 12:14, 2 May 2008

Template:STRUCTURE 1elk

VHS domain of TOM1 protein from H. sapiens


Overview

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.

About this Structure

1ELK is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

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 Page seeded by OCA on Fri May 2 15:14:56 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools