1q1o: Difference between revisions

Revision as of 10:11, 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:1q1o.png

Template:STRUCTURE 1q1o

Solution Structure of the PB1 Domain of Cdc24p (Long Form)Solution Structure of the PB1 Domain of Cdc24p (Long Form)

Template:ABSTRACT PUBMED 14517229

About this StructureAbout this Structure

1Q1O is a Single protein structure of sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA.

ReferenceReference

The PB1 domain and the PC motif-containing region are structurally similar protein binding modules., Yoshinaga S, Kohjima M, Ogura K, Yokochi M, Takeya R, Ito T, Sumimoto H, Inagaki F, EMBO J. 2003 Oct 1;22(19):4888-97. PMID:14517229

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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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 {{STRUCTURE_1q1o|  PDB=1q1o  |  SCENE=  }}
-'''Solution Structure of the PB1 Domain of Cdc24p (Long Form)'''
+===Solution Structure of the PB1 Domain of Cdc24p (Long Form)===
-==Overview==
+<!--
-The PC motif is evolutionarily conserved together with the PB1 domain, a binding partner of the PC motif-containing protein. For interaction with the PB1 domain, the PC motif-containing region (PCCR) comprising the PC motif and its flanking regions is required. Because the PB1 domain and the PCCR are novel binding modules found in a variety of signaling proteins, their structural and functional characterization is crucial. Bem1p and Cdc24p interact through the PB1-PCCR interaction and regulate cell polarization in budding yeast. Here, we determined a tertiary structure of the PCCR of Cdc24p by NMR. The tertiary structure of the PCCR is similar to that of the PB1 domain of Bem1p, which is classified into a ubiquitin fold. The PC motif portion takes a compact betabetaalpha-fold, presented on the ubiquitin scaffold. Mutational studies indicate that the PB1-PCCR interaction is mainly electrostatic. Based on the structural information, we group the PB1 domains and the PCCRs into a novel family, named the PB1 family. Thus, the PB1 family proteins form a specific dimer with each other.
+The line below this paragraph, {{ABSTRACT_PUBMED_14517229}}, adds the Publication Abstract to the page
+(as it appears on PubMed at http://www.pubmed.gov), where 14517229 is the PubMed ID number.
+-->
+{{ABSTRACT_PUBMED_14517229}}
 ==About this Structure==
-Q1O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1O OCA].
+Q1O is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1Q1O OCA].
 ==Reference==
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 [[Category: Protein-protein interaction]]
 [[Category: Yeast]]
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