1n42

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[[Image:1n42.gif|left|200px]]
 
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==Crystal Structure of Annexin V R149E Mutant==
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The line below this paragraph, containing "STRUCTURE_1n42", creates the "Structure Box" on the page.
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<StructureSection load='1n42' size='340' side='right'caption='[[1n42]], [[Resolution|resolution]] 2.10&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'>[[1n42]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N42 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N42 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]] 2.1&#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>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
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{{STRUCTURE_1n42| PDB=1n42 | 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=1n42 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n42 OCA], [https://pdbe.org/1n42 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n42 RCSB], [https://www.ebi.ac.uk/pdbsum/1n42 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n42 ProSAT]</span></td></tr>
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</table>
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== Function ==
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[https://www.uniprot.org/uniprot/ANXA5_RAT ANXA5_RAT] This protein is an anticoagulant protein that acts as an indirect inhibitor of the thromboplastin-specific complex, which is involved in the blood coagulation cascade.
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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/n4/1n42_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=1n42 ConSurf].
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<div style="clear:both"></div>
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'''Crystal Structure of Annexin V R149E Mutant'''
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==See Also==
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*[[Annexin|Annexin]]
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*[[Annexin 3D structures|Annexin 3D structures]]
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==Overview==
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__TOC__
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Annexin V is an abundant eukaryotic protein that binds phospholipid membranes in a Ca(2+)-dependent manner. In the present studies, site-directed mutagenesis was combined with x-ray crystallography and solution liposome binding assays to probe the functional role of a cluster of interfacial basic residues in annexin V. Four mutants were investigated: R23E, K27E, R61E, and R149E. All four mutants exhibited a significant reduction in adsorption to phospholipid membranes relative to the wild-type protein, and the R23E mutation was the most deleterious. Crystal structures of wild-type and mutant proteins were similar except for local changes in salt bridges involving basic cluster residues. The combined data indicate that Arg(23) is a major determinant for interfacial phospholipid binding and participates in an intermolecular salt bridge that is key for trimer formation on the membrane surface. Together, crystallographic and solution data provide evidence that the interfacial basic cluster is a locus where trimerization is synergistically coupled to membrane phospholipid binding.
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</StructureSection>
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[[Category: Large Structures]]
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==About this Structure==
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1N42 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N42 OCA].
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==Reference==
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Interfacial basic cluster in annexin V couples phospholipid binding and trimer formation on membrane surfaces., Mo Y, Campos B, Mealy TR, Commodore L, Head JF, Dedman JR, Seaton BA, J Biol Chem. 2003 Jan 24;278(4):2437-43. Epub 2002 Oct 24. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12401794 12401794]
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[[Category: Rattus norvegicus]]
[[Category: Rattus norvegicus]]
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[[Category: Single protein]]
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[[Category: Campos B]]
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[[Category: Campos, B.]]
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[[Category: Commodore L]]
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[[Category: Commodore, L.]]
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[[Category: Dedman JR]]
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[[Category: Dedman, J R.]]
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[[Category: Head JF]]
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[[Category: Head, J F.]]
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[[Category: Mealy TR]]
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[[Category: Mealy, T R.]]
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[[Category: Mo YD]]
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[[Category: Mo, Y D.]]
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[[Category: Seaton BA]]
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[[Category: Seaton, B A.]]
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[[Category: Calcium]]
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[[Category: Membrane binding protein]]
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[[Category: Phospholipid]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 02:03:56 2008''
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Current revision

Crystal Structure of Annexin V R149E Mutant

PDB ID 1n42

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