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1ip9

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SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P

Structural highlights

1ip9 is a 1 chain structure with sequence from Saccharomyces cerevisiae. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	Solution NMR
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

BEM1_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 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^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Gao XD, Sperber LM, Kane SA, Tong Z, Tong AH, Boone C, Bi E. Sequential and distinct roles of the cadherin domain-containing protein Axl2p in cell polarization in yeast cell cycle. Mol Biol Cell. 2007 Jul;18(7):2542-60. Epub 2007 Apr 25. PMID:17460121 doi:http://dx.doi.org/10.1091/mbc.E06-09-0822
↑ Terasawa H, Noda Y, Ito T, Hatanaka H, Ichikawa S, Ogura K, Sumimoto H, Inagaki F. Structure and ligand recognition of the PB1 domain: a novel protein module binding to the PC motif. EMBO J. 2001 Aug 1;20(15):3947-56. PMID:11483498 doi:10.1093/emboj/20.15.3947

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1ip9"

@@ Line 1: / Line 1: @@
 ==SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P==
-<StructureSection load='1ip9' size='340' side='right'caption='[[1ip9]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
+<StructureSection load='1ip9' size='340' side='right'caption='[[1ip9]]' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1ip9]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Atcc_18824 Atcc 18824]. 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 [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1IP9 FirstGlance]. <br>
+<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='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[1ipg|1ipg]]</td></tr>
+</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'>[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://pdbe.org/1ip9 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1ip9 RCSB], [http://www.ebi.ac.uk/pdbsum/1ip9 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1ip9 ProSAT]</span></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 ==
-[[http://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>
+[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]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Atcc 18824]]
 [[Category: Large Structures]]
-[[Category: Hatanaka, H]]
+[[Category: Saccharomyces cerevisiae]]
-[[Category: Ichikawa, S]]
+[[Category: Hatanaka H]]
-[[Category: Inagaki, F]]
+[[Category: Ichikawa S]]
-[[Category: Ito, T]]
+[[Category: Inagaki F]]
-[[Category: Noda, Y]]
+[[Category: Ito T]]
-[[Category: Ogura, K]]
+[[Category: Noda Y]]
-[[Category: Sumimoto, H]]
+[[Category: Ogura K]]
-[[Category: Terasawa, H]]
+[[Category: Sumimoto H]]
-[[Category: Signaling protein]]
+[[Category: Terasawa H]]
-[[Category: Ubiquitin alpha/beta roll]]

1ip9

From Proteopedia

Current revision

SOLUTION STRUCTURE OF THE PB1 DOMAIN OF BEM1P

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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