1o06: Difference between revisions

Revision as of 12:58, 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:1o06.png

Template:STRUCTURE 1o06

Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)

Template:ABSTRACT PUBMED 12750381

About this StructureAbout this Structure

1O06 is a Single protein structure. Full crystallographic information is available from OCA.

ReferenceReference

Structure and ubiquitin binding of the ubiquitin-interacting motif., Fisher RD, Wang B, Alam SL, Higginson DS, Robinson H, Sundquist WI, Hill CP, J Biol Chem. 2003 Aug 1;278(31):28976-84. Epub 2003 May 14. PMID:12750381

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

OCA

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-'''Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)'''
+===Crystal structure of the Vps27p Ubiquitin Interacting Motif (UIM)===
-==Overview==
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-Ubiquitylation is used to target proteins into a large number of different biological processes including proteasomal degradation, endocytosis, virus budding, and vacuolar protein sorting (Vps). Ubiquitylated proteins are typically recognized using one of several different conserved ubiquitin binding modules. Here, we report the crystal structure and ubiquitin binding properties of one such module, the ubiquitin-interacting motif (UIM). We found that UIM peptides from several proteins involved in endocytosis and vacuolar protein sorting including Hrs, Vps27p, Stam1, and Eps15 bound specifically, but with modest affinity (Kd = 0.1-1 mm), to free ubiquitin. Full affinity ubiquitin binding required the presence of conserved acidic patches at the N and C terminus of the UIM, as well as highly conserved central alanine and serine residues. NMR chemical shift perturbation mapping experiments demonstrated that all of these UIM peptides bind to the I44 surface of ubiquitin. The 1.45 A resolution crystal structure of the second yeast Vps27p UIM (Vps27p-2) revealed that the ubiquitin-interacting motif forms an amphipathic helix. Although Vps27p-2 is monomeric in solution, the motif unexpectedly crystallized as an antiparallel four-helix bundle, and the potential biological implications of UIM oligomerization are therefore discussed.
+The line below this paragraph, {{ABSTRACT_PUBMED_12750381}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_12750381}}
 ==About this Structure==
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