1vd2: Difference between revisions

Revision as of 05:04, 28 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:1vd2.png

Template:STRUCTURE 1vd2

Solution Structure of the PB1 domain of PKCiotaSolution Structure of the PB1 domain of PKCiota

Template:ABSTRACT PUBMED 15143057

About this StructureAbout this Structure

1VD2 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

ReferenceReference

Solution structure of atypical protein kinase C PB1 domain and its mode of interaction with ZIP/p62 and MEK5., Hirano Y, Yoshinaga S, Ogura K, Yokochi M, Noda Y, Sumimoto H, Inagaki F, J Biol Chem. 2004 Jul 23;279(30):31883-90. Epub 2004 May 13. PMID:15143057

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-'''Solution Structure of the PB1 domain of PKCiota'''
+===Solution Structure of the PB1 domain of PKCiota===
-==Overview==
+<!--
-Atypical protein kinase C (aPKC) has been implicated in several signaling pathways such as cell polarity, cell survival, and cell differentiation. In contrast to other PKCs, aPKC is unique in having the PB1 (Phox and Bem 1) domain in the N terminus. The aPKC PB1 domain binds with ZIP/p62, Par6, or MEK5 through a PB1-PB1 domain interaction that controls the localization of aPKC. Here, we determined the three-dimensional structure of the PB1 domain of PKCiota by NMR and found that the PB1 domain adopts a ubiquitin fold. The OPCA (OPR, PC, and AID) motif inserted into the ubiquitin fold was presented as a betabetaalpha fold in which the side chains of conserved Asp residues were oriented to the same direction to form an acidic surface. This structural feature suggested that the acidic surface of the PKCiota PB1 domain interacted with the basic surface of the target PB1 domains, and this was confirmed in the case of the PKCiota-ZIP/p62 complex by mutational analysis. Interestingly, in the PKCiota PB1 domain a conserved lysine residue was located on the side opposite to the OPCA motif-presenting surface, suggesting dual roles for the PKCiota PB1 domain in that it could interact with either the conserved lysine residue or the acidic residues on the OPCA motif of the target PB1 domains.
+The line below this paragraph, {{ABSTRACT_PUBMED_15143057}}, adds the Publication Abstract to the page
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+{{ABSTRACT_PUBMED_15143057}}
 ==About this Structure==
-VD2 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=1VD2 OCA].
+VD2 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=1VD2 OCA].
 ==Reference==
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 [[Category: Pb1 domain]]
 [[Category: Zip/p62]]
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