1n41

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[[Image:1n41.gif|left|200px]]<br /><applet load="1n41" size="350" color="white" frame="true" align="right" spinBox="true"
 
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caption="1n41, resolution 2.1&Aring;" />
 
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'''Crystal Structure of Annexin V K27E Mutant'''<br />
 
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==Overview==
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==Crystal Structure of Annexin V K27E Mutant==
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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 load='1n41' size='340' side='right'caption='[[1n41]], [[Resolution|resolution]] 2.10&Aring;' scene=''>
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== Structural highlights ==
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<table><tr><td colspan='2'>[[1n41]] 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=1N41 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1N41 FirstGlance]. <br>
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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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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1n41 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1n41 OCA], [https://pdbe.org/1n41 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1n41 RCSB], [https://www.ebi.ac.uk/pdbsum/1n41 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1n41 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/n4/1n41_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=1n41 ConSurf].
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<div style="clear:both"></div>
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==About this Structure==
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==See Also==
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1N41 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1N41 OCA].
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*[[Annexin 3D structures|Annexin 3D structures]]
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__TOC__
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==Reference==
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</StructureSection>
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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://ispc.weizmann.ac.il//pmbin/getpm?pmid=12401794 12401794]
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[[Category: Large Structures]]
[[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: CA]]
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[[Category: SO4]]
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[[Category: calcium]]
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[[Category: phospholipid membrane binding protein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:02:03 2008''
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Current revision

Crystal Structure of Annexin V K27E Mutant

PDB ID 1n41

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