2f2p

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{{Seed}}
 
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[[Image:2f2p.png|left|200px]]
 
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==Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode==
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The line below this paragraph, containing "STRUCTURE_2f2p", creates the "Structure Box" on the page.
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<StructureSection load='2f2p' size='340' side='right'caption='[[2f2p]], [[Resolution|resolution]] 2.60&Aring;' scene=''>
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You may change the PDB parameter (which sets the PDB file loaded into the applet)
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== Structural highlights ==
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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<table><tr><td colspan='2'>[[2f2p]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2P OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=2F2P FirstGlance]. <br>
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or leave the SCENE parameter empty for the default display.
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</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.6&#8491;</td></tr>
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<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene></td></tr>
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{{STRUCTURE_2f2p| PDB=2f2p | SCENE= }}
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=2f2p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=2f2p OCA], [https://pdbe.org/2f2p PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=2f2p RCSB], [https://www.ebi.ac.uk/pdbsum/2f2p PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=2f2p ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/PP2BA_BOVIN PP2BA_BOVIN] Calcium-dependent, calmodulin-stimulated protein phosphatase. This subunit may have a role in the calmodulin activation of calcineurin. Dephosphorylates DNM1L, HSPB1 and SSH1 (By similarity).[https://www.uniprot.org/uniprot/CALM_BOVIN CALM_BOVIN] Calmodulin mediates the control of a large number of enzymes, ion channels and other proteins by Ca(2+). Among the enzymes to be stimulated by the calmodulin-Ca(2+) complex are a number of protein kinases and phosphatases. Together with CEP110 and centrin, is involved in a genetic pathway that regulates the centrosome cycle and progression through cytokinesis (By similarity).
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== Evolutionary Conservation ==
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[[Image:Consurf_key_small.gif|200px|right]]
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Check<jmol>
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<jmolCheckbox>
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<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/f2/2f2p_consurf.spt"</scriptWhenChecked>
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<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
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<text>to colour the structure by Evolutionary Conservation</text>
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</jmolCheckbox>
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</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=2f2p ConSurf].
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<div style="clear:both"></div>
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<div style="background-color:#fffaf0;">
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== Publication Abstract from PubMed ==
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Calcineurin is a calmodulin-binding protein in brain and the only serine/threonine protein phosphatase under the control of Ca2+/calmodulin (CaM), which plays a critical role in coupling Ca2+ signals to cellular responses. CaM up-regulates the phosphatase activity of calcineurin by binding to the CaM-binding domain (CBD) of calcineurin subunit A. Here, we report crystal structural studies of CaM bound to a CBD peptide. The chimeric protein containing CaM and the CBD peptide forms an intimate homodimer, in which CaM displays a native-like extended conformation and the CBD peptide shows alpha-helical structure. Unexpectedly, the N-terminal lobe from one CaM and the C-terminal lobe from the second molecule form a combined binding site to trap the peptide. Thus, the dimer provides two binding sites, each of which is reminiscent of the fully collapsed conformation of CaM commonly observed in complex with, for example, the myosin light chain kinase (MLCK) peptide. The interaction between the peptide and CaM is highly specific and similar to MLCK.
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===Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode===
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Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode.,Ye Q, Li X, Wong A, Wei Q, Jia Z Biochemistry. 2006 Jan 24;45(3):738-45. PMID:16411749<ref>PMID:16411749</ref>
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From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
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</div>
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<div class="pdbe-citations 2f2p" style="background-color:#fffaf0;"></div>
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==See Also==
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The line below this paragraph, {{ABSTRACT_PUBMED_16411749}}, adds the Publication Abstract to the page
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*[[Calmodulin 3D structures|Calmodulin 3D structures]]
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(as it appears on PubMed at http://www.pubmed.gov), where 16411749 is the PubMed ID number.
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== References ==
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<references/>
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{{ABSTRACT_PUBMED_16411749}}
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__TOC__
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</StructureSection>
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==About this Structure==
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2F2P is a 2 chains structure of sequences from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2F2P OCA].
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==Reference==
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<ref group="xtra">PMID:16411749</ref><references group="xtra"/>
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[[Category: Bos taurus]]
[[Category: Bos taurus]]
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[[Category: Jia, Z.]]
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[[Category: Large Structures]]
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[[Category: Wong, A.]]
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[[Category: Jia Z]]
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[[Category: Ye, Q.]]
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[[Category: Wong A]]
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[[Category: Calcineurin]]
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[[Category: Ye Q]]
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[[Category: Calcium]]
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[[Category: Calmodulin]]
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[[Category: Ef-hand]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Tue Feb 17 02:48:36 2009''
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Current revision

Structure of calmodulin bound to a calcineurin peptide: a new way of making an old binding mode

PDB ID 2f2p

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