View source for 1ip9

[[Image:1ip9.jpg|left|200px]]<br /><applet load="1ip9" size="450" color="white" frame="true" align="right" spinBox="true" 
caption="1ip9" />
'''SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P'''<br />

==Overview==
PB1 domains are novel protein modules capable of binding to target, proteins that contain PC motifs. We report here the NMR structure and, ligand-binding site of the PB1 domain of the cell polarity establishment, protein, Bem1p. In addition, we identify the topology of the PC, motif-containing region of Cdc24p by NMR, another cell polarity, establishment protein that interacts with Bem1p. The PC motif-containing, region is a structural domain offering a scaffold to the PC motif. The, chemical shift perturbation experiment and the mutagenesis study show that, the PC motif is a major structural element that binds to the PB1 domain. A, structural database search reveals close similarity between the Bem1p PB1, domain and the c-Raf1 Ras-binding domain. However, these domains are, functionally distinct from each other.

==About this Structure==
1IP9 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=1IP9 OCA]. 

==Reference==
Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif., Terasawa H, Noda Y, Ito T, Hatanaka H, Ichikawa S, Ogura K, Sumimoto H, Inagaki F, EMBO J. 2001 Aug 1;20(15):3947-56. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=11483498 11483498]
[[Category: Saccharomyces cerevisiae]]
[[Category: Single protein]]
[[Category: Hatanaka, H.]]
[[Category: Ichikawa, S.]]
[[Category: Inagaki, F.]]
[[Category: Ito, T.]]
[[Category: Noda, Y.]]
[[Category: Ogura, K.]]
[[Category: Sumimoto, H.]]
[[Category: Terasawa, H.]]
[[Category: ubiquitin alpha/beta roll]]

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