1wmh: Difference between revisions

Revision as of 15:05, 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:1wmh.png

Template:STRUCTURE 1wmh

Crystal structure of a PB1 domain complex of Protein kinase c iota and Par6 alphaCrystal structure of a PB1 domain complex of Protein kinase c iota and Par6 alpha

Template:ABSTRACT PUBMED 15590654

About this StructureAbout this Structure

1WMH is a Protein complex structure of sequences from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of a cell polarity regulator, a complex between atypical PKC and Par6 PB1 domains., Hirano Y, Yoshinaga S, Takeya R, Suzuki NN, Horiuchi M, Kohjima M, Sumimoto H, Inagaki F, J Biol Chem. 2005 Mar 11;280(10):9653-61. Epub 2004 Dec 7. PMID:15590654

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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 a PB1 domain complex of Protein kinase c iota and Par6 alpha'''
+===Crystal structure of a PB1 domain complex of Protein kinase c iota and Par6 alpha===
-==Overview==
+<!--
-A complex of atypical PKC and Par6 is a common regulator for cell polarity-related processes, which is an essential clue to evolutionary conserved cell polarity regulation. Here, we determined the crystal structure of the complex of PKCiota and Par6alpha PB1 domains to a resolution of 1.5 A. Both PB1 domains adopt a ubiquitin fold. PKCiota PB1 presents an OPR, PC, and AID (OPCA) motif, 28 amino acid residues with acidic and hydrophobic residues, which interacts with the conserved lysine residue of Par6alpha PB1 in a front and back manner. On the interface, several salt bridges are formed including the conserved acidic residues on the OPCA motif of PKCiota PB1 and the conserved lysine residue on the Par6alpha PB1. Structural comparison of the PKCiota and Par6alpha PB1 complex with the p40phox and p67phox PB1 domain complex, subunits of neutrophil NADPH oxidase, reveals that the specific interaction is achieved by tilting the interface so that the insertion or extension in the sequence is engaged in the specificity determinant. The PB1 domain develops the interaction surface on the ubiquitin fold to increase the versatility of molecular interaction.
+The line below this paragraph, {{ABSTRACT_PUBMED_15590654}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 15590654 is the PubMed ID number.
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+{{ABSTRACT_PUBMED_15590654}}
 ==About this Structure==
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 [[Category: Par6]]
 [[Category: Pb1 domain]]
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