1ip9: Difference between revisions
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|RELATEDENTRY=[[1ipg|1IPG]] | |||
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ip9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ip9 OCA], [http://www.ebi.ac.uk/pdbsum/1ip9 PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ip9 RCSB]</span> | |||
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[[Category: ubiquitin alpha/beta roll]] | [[Category: ubiquitin alpha/beta roll]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 21:22:50 2008'' | ||
Revision as of 21:22, 30 March 2008
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| Related: | 1IPG
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| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P
OverviewOverview
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 StructureAbout this Structure
1IP9 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.
ReferenceReference
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:11483498
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