1wr0: Difference between revisions

Revision as of 18:12, 27 July 2008

This article has been automatically seeded. Changes to this page should pertain to the PDB entry only and not to the protein or biomolecule in general.

File:1wr0.png

Template:STRUCTURE 1wr0

Structural characterization of the MIT domain from human Vps4bStructural characterization of the MIT domain from human Vps4b

Template:ABSTRACT PUBMED 16018968

About this StructureAbout this Structure

1WR0 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Structural characterization of the MIT domain from human Vps4b., Takasu H, Jee JG, Ohno A, Goda N, Fujiwara K, Tochio H, Shirakawa M, Hiroaki H, Biochem Biophys Res Commun. 2005 Aug 26;334(2):460-5. PMID:16018968

Page seeded by OCA on Sun Jul 27 18:12:00 2008

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA

@@ Line 1: / Line 1: @@
-[[Image:1wr0.gif|left|200px]]
+{{Seed}}
+[[Image:1wr0.png|left|200px]]
 <!--
@@ Line 9: / Line 10: @@
 {{STRUCTURE_1wr0|  PDB=1wr0  |  SCENE=  }}
-'''Structural characterization of the MIT domain from human Vps4b'''
+===Structural characterization of the MIT domain from human Vps4b===
-==Overview==
+<!--
-The microtubule interacting and trafficking (MIT) domain is a small protein module of unknown function that is conserved in proteins of diverse function, such as Vps4, sorting nexin 15 (SNX15), and spastin. One non-synonymous single nucleotide polymorphism was reported, which results in a Ile58-to-Met (I58M) substitution in hVps4b. Here, we have determined the solution structure of the MIT domain isolated from the NH(2)-terminus of human Vps4b, an AAA-ATPase involved in multivesicular body formation. The MIT domain adopts an 'up-and-down' three-helix bundle. Comparison with the sequences of other MIT domains clearly shows that the residues involved in inter-helical contacts are well conserved. The Ile58-to-Met substitution resulted a substantial thermal instability. In addition, we found a shallow crevice between helices A and C that may serve as a protein-binding site. We propose that the MIT domain serves as a putative adaptor domain for the ESCRT-III complex involved in endosomal trafficking.
+The line below this paragraph, {{ABSTRACT_PUBMED_16018968}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 16018968 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_16018968}}
 ==About this Structure==
-WR0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WR0 OCA].
+WR0 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1WR0 OCA].
 ==Reference==
@@ Line 43: / Line 47: @@
 [[Category: Structural genomic]]
 [[Category: Vps4b]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 14:02:02 2008''
+''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 18:12:00 2008''