3bd0

From Proteopedia

(Difference between revisions)

Revision as of 08:00, 25 October 2017

Crystal structure of Memo, form II

Structural highlights

3bd0 is a 4 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:
Related:	3bcz
Gene:	MEMO1, C2orf4, NS5ATP7 (HUMAN)
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[MEMO1_HUMAN] May control cell migration by relaying extracellular chemotactic signals to the microtubule cytoskeleton. Mediator of ERBB2 signaling. The MEMO1-RHOA-DIAPH1 signaling pathway plays an important role in ERBB2-dependent stabilization of microtubules at the cell cortex. It controls the localization of APC and CLASP2 to the cell membrane, via the regulation of GSK3B activity. In turn, membrane-bound APC allows the localization of the MACF1 to the cell membrane, which is required for microtubule capture and stabilization. Is required for breast carcinoma cell migration.^[1] ^[2]

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

Memo (mediator of ErbB2-driven cell motility) is a 297-amino-acid protein recently shown to co-precipitate with the C terminus of ErbB2 and be required for ErbB2-driven cell motility. Memo is not homologous to any known signaling proteins, and how it mediates ErbB2 signals is not known. To provide a molecular basis for understanding Memo function, we have determined and report here the 2.1A crystal structure of human Memo and show it be homologous to class III nonheme iron-dependent dioxygenases, a structural class that now includes a zinc-binding protein of unknown function. No metal binding or enzymatic activity can be detected for Memo, but Memo does bind directly to a specific ErbB2-derived phosphopeptide encompassing Tyr-1227 using its vestigial enzymatic active site. Memo thus represents a new class of phosphotyrosine-binding protein.

Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-derived phosphopeptide in its vestigial active site.,Qiu C, Lienhard S, Hynes NE, Badache A, Leahy DJ J Biol Chem. 2008 Feb 1;283(5):2734-40. Epub 2007 Nov 28. PMID:18045866^[3]

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

References

↑ Marone R, Hess D, Dankort D, Muller WJ, Hynes NE, Badache A. Memo mediates ErbB2-driven cell motility. Nat Cell Biol. 2004 Jun;6(6):515-22. Epub 2004 May 23. PMID:15156151 doi:http://dx.doi.org/10.1038/ncb1134
↑ Zaoui K, Benseddik K, Daou P, Salaun D, Badache A. ErbB2 receptor controls microtubule capture by recruiting ACF7 to the plasma membrane of migrating cells. Proc Natl Acad Sci U S A. 2010 Oct 26;107(43):18517-22. doi:, 10.1073/pnas.1000975107. Epub 2010 Oct 11. PMID:20937854 doi:10.1073/pnas.1000975107
↑ Qiu C, Lienhard S, Hynes NE, Badache A, Leahy DJ. Memo is homologous to nonheme iron dioxygenases and binds an ErbB2-derived phosphopeptide in its vestigial active site. J Biol Chem. 2008 Feb 1;283(5):2734-40. Epub 2007 Nov 28. PMID:18045866 doi:http://dx.doi.org/10.1074/jbc.M703523200

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/3bd0"

Categories: Human | Qiu, C | Alpha/beta structure | Peptide binding protein

@@ Line 1: / Line 1: @@
 ==Crystal structure of Memo, form II==
 <StructureSection load='3bd0' size='340' side='right' caption='[[3bd0]], [[Resolution|resolution]] 3.01&Aring;' scene=''>
@@ Line 6: / Line 7: @@
 <tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat">[[3bcz|3bcz]]</td></tr>
 <tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">MEMO1, C2orf4, NS5ATP7 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=3bd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bd0 OCA], [http://pdbe.org/3bd0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bd0 RCSB], [http://www.ebi.ac.uk/pdbsum/3bd0 PDBsum]</span></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=3bd0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3bd0 OCA], [http://pdbe.org/3bd0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3bd0 RCSB], [http://www.ebi.ac.uk/pdbsum/3bd0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3bd0 ProSAT]</span></td></tr>
 </table>
 == Function ==

3bd0

From Proteopedia

Revision as of 08:00, 25 October 2017

Crystal structure of Memo, form II

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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