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New page: left|200px<br /><applet load="1pqs" size="450" color="white" frame="true" align="right" spinBox="true" caption="1pqs" /> '''Solution structure of the C-terminal OPCA do...
 
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[[Image:1pqs.gif|left|200px]]<br /><applet load="1pqs" size="450" color="white" frame="true" align="right" spinBox="true"  
[[Image:1pqs.gif|left|200px]]<br /><applet load="1pqs" size="350" color="white" frame="true" align="right" spinBox="true"  
caption="1pqs" />
caption="1pqs" />
'''Solution structure of the C-terminal OPCA domain of yCdc24p'''<br />
'''Solution structure of the C-terminal OPCA domain of yCdc24p'''<br />


==Overview==
==Overview==
Phox and Bem1 (PB1) domains mediate protein-protein interactions via the, formation of homo- or hetero-dimers. The C-terminal PB1 domain of yeast, cell division cycle 24 (CDC24p), a guanine-nucleotide exchange factor, involved in cell polarity establishment, is known to interact with the PB1, domain occurring in bud emergence MSB1 interacting 1 (BEM1p) during the, regulation of the yeast budding process via its OPR/PC/AID (OPCA) motif., Here, we present the structure of an N-terminally truncated version of the, Sc CDC24p PB1 domain. It shows a different topology of the beta-sheet than, the long form. However, the C-terminal part of the structure shows the, conserved PB1 domain features including the OPCA motif with a slight, rearrangement of helix alpha1. Residues which are important for the, heterodimerization with BEM1p are structurally preserved.
Phox and Bem1 (PB1) domains mediate protein-protein interactions via the formation of homo- or hetero-dimers. The C-terminal PB1 domain of yeast cell division cycle 24 (CDC24p), a guanine-nucleotide exchange factor involved in cell polarity establishment, is known to interact with the PB1 domain occurring in bud emergence MSB1 interacting 1 (BEM1p) during the regulation of the yeast budding process via its OPR/PC/AID (OPCA) motif. Here, we present the structure of an N-terminally truncated version of the Sc CDC24p PB1 domain. It shows a different topology of the beta-sheet than the long form. However, the C-terminal part of the structure shows the conserved PB1 domain features including the OPCA motif with a slight rearrangement of helix alpha1. Residues which are important for the heterodimerization with BEM1p are structurally preserved.


==About this Structure==
==About this Structure==
1PQS is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1PQS OCA].  
1PQS is a [http://en.wikipedia.org/wiki/Single_protein 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=1PQS OCA].  


==Reference==
==Reference==
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[[Category: Leitner, D.]]
[[Category: Leitner, D.]]
[[Category: Oschkinat, H.]]
[[Category: Oschkinat, H.]]
[[Category: Pires, J.R.]]
[[Category: Pires, J R.]]
[[Category: Schmieder, P.]]
[[Category: Schmieder, P.]]
[[Category: Wahl, M.]]
[[Category: Wahl, M.]]
[[Category: alpha and beta protein]]
[[Category: alpha and beta protein]]


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