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New page: left|200px<br /><applet load="1uzc" size="450" color="white" frame="true" align="right" spinBox="true" caption="1uzc" /> '''THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYP... |
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== | ==THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11== | ||
The FF domain is a 60 amino acid residue phosphopeptide-binding module | <StructureSection load='1uzc' size='340' side='right'caption='[[1uzc]]' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[1uzc]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. This structure supersedes the now removed PDB entry [http://oca.weizmann.ac.il/oca-bin/send-pdb?obs=1&id=1h40 1h40]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1UZC OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1UZC 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=1uzc FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1uzc OCA], [https://pdbe.org/1uzc PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1uzc RCSB], [https://www.ebi.ac.uk/pdbsum/1uzc PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1uzc ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/PR40A_HUMAN PR40A_HUMAN] Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.<ref>PMID:21834987</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/uz/1uzc_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=1uzc ConSurf]. | |||
<div style="clear:both"></div> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
The FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 and p190RHOGAP. We have determined the structure of an FF domain from HYPA/FBP11. The domain is composed of three alpha helices arranged in an orthogonal bundle with a 3(10) helix in the loop between the second and third alpha helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold. | |||
The structure of an FF domain from human HYPA/FBP11.,Allen M, Friedler A, Schon O, Bycroft M J Mol Biol. 2002 Oct 25;323(3):411-6. PMID:12381297<ref>PMID:12381297</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 1uzc" style="background-color:#fffaf0;"></div> | |||
== References == | |||
<references/> | |||
__TOC__ | |||
</StructureSection> | |||
[[Category: Homo sapiens]] | [[Category: Homo sapiens]] | ||
[[Category: | [[Category: Large Structures]] | ||
[[Category: Allen | [[Category: Allen MD]] | ||
[[Category: Bycroft | [[Category: Bycroft M]] | ||
[[Category: Friedler | [[Category: Friedler A]] | ||
[[Category: Jemth | [[Category: Jemth P]] | ||
[[Category: Schon | [[Category: Schon O]] | ||
Latest revision as of 16:23, 9 May 2024
THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11THE STRUCTURE OF AN FF DOMAIN FROM HUMAN HYPA/FBP11
Structural highlights
FunctionPR40A_HUMAN Binds to WASL/N-WASP and suppresses its translocation from the nucleus to the cytoplasm, thereby inhibiting its cytoplasmic function (By similarity). Plays a role in the regulation of cell morphology and cytoskeletal organization. Required in the control of cell shape and migration. May play a role in cytokinesis. May be involved in pre-mRNA splicing.[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 PubMedThe FF domain is a 60 amino acid residue phosphopeptide-binding module found in a variety of eukaryotic proteins including the transcription elongation factor CA150, the splicing factor Prp40 and p190RHOGAP. We have determined the structure of an FF domain from HYPA/FBP11. The domain is composed of three alpha helices arranged in an orthogonal bundle with a 3(10) helix in the loop between the second and third alpha helices. The structure differs from those of other phosphopeptide-binding domains and represents a novel phosphopeptide-binding fold. The structure of an FF domain from human HYPA/FBP11.,Allen M, Friedler A, Schon O, Bycroft M J Mol Biol. 2002 Oct 25;323(3):411-6. PMID:12381297[2] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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