1ip9: Difference between revisions
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< | ==SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P== | ||
<StructureSection load='1ip9' size='340' side='right'caption='[[1ip9]]' scene=''> | |||
You may | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1ip9]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1IP9 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1IP9 FirstGlance]. <br> | |||
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</td></tr> | |||
-- | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ip9 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ip9 OCA], [https://pdbe.org/1ip9 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ip9 RCSB], [https://www.ebi.ac.uk/pdbsum/1ip9 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ip9 ProSAT]</span></td></tr> | ||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/BEM1_YEAST BEM1_YEAST] Necessary for cell polarization during vegetative growth. May link the cytoskeleton to morphogenic determinants on the cell surface.<ref>PMID:17460121</ref> | |||
== Evolutionary Conservation == | |||
[[Image:Consurf_key_small.gif|200px|right]] | |||
Check<jmol> | |||
<jmolCheckbox> | |||
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ip/1ip9_consurf.spt"</scriptWhenChecked> | |||
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked> | |||
<text>to colour the structure by Evolutionary Conservation</text> | |||
</jmolCheckbox> | |||
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=1ip9 ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
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. | |||
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<ref>PMID:11483498</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1ip9" style="background-color:#fffaf0;"></div> | |||
== References == | |||
--> | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
== | [[Category: Large Structures]] | ||
[[Category: Saccharomyces cerevisiae]] | [[Category: Saccharomyces cerevisiae]] | ||
[[Category: Hatanaka H]] | |||
[[Category: Hatanaka | [[Category: Ichikawa S]] | ||
[[Category: Ichikawa | [[Category: Inagaki F]] | ||
[[Category: Inagaki | [[Category: Ito T]] | ||
[[Category: Ito | [[Category: Noda Y]] | ||
[[Category: Noda | [[Category: Ogura K]] | ||
[[Category: Ogura | [[Category: Sumimoto H]] | ||
[[Category: Sumimoto | [[Category: Terasawa H]] | ||
[[Category: Terasawa | |||
Latest revision as of 02:34, 28 December 2023
SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1PSOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P
Structural highlights
FunctionBEM1_YEAST Necessary for cell polarization during vegetative growth. May link the cytoskeleton to morphogenic determinants on the cell surface.[1] Evolutionary Conservation Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf. Publication Abstract from PubMedPB1 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. 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[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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