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1pqs

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(New page: 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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'''Solution structure of the C-terminal OPCA domain of yCdc24p'''<br />
'''Solution structure of the C-terminal OPCA domain of yCdc24p'''<br />
==Overview==
==Overview==
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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.
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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==
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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].
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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.]]
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[[Category: Pires, J.R.]]
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[[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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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Wed Nov 21 00:02:17 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:31:33 2008''

Revision as of 12:31, 21 February 2008


1pqs

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Solution structure of the C-terminal OPCA domain of yCdc24p

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.

About this Structure

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

Reference

The solution structure of an N-terminally truncated version of the yeast CDC24p PB1 domain shows a different beta-sheet topology., Leitner D, Wahl M, Labudde D, Krause G, Diehl A, Schmieder P, Pires JR, Fossi M, Wiedemann U, Leidert M, Oschkinat H, FEBS Lett. 2005 Jul 4;579(17):3534-8. PMID:15961083

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