1bcz: Difference between revisions

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-[[Image:1bcz.jpg|left|200px]]
- {{Structure
+==RECOMBINANT RAT ANNEXIN V, T72S MUTANT==
-|PDB= 1bcz |SIZE=350|CAPTION= <scene name='initialview01'>1bcz</scene>, resolution 2.2&Aring;
+<StructureSection load='1bcz' size='340' side='right'caption='[[1bcz]], [[Resolution|resolution]] 2.20&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene> and <scene name='pdbligand=SO4:SULFATE ION'>SO4</scene>
+<table><tr><td colspan='2'>[[1bcz]] 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=1BCZ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1BCZ FirstGlance]. <br>
-|ACTIVITY=
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.2&#8491;</td></tr>
-|GENE=
+<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>
-}}
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1bcz FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1bcz OCA], [https://pdbe.org/1bcz PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1bcz RCSB], [https://www.ebi.ac.uk/pdbsum/1bcz PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1bcz ProSAT]</span></td></tr>
+</table>
+== Function ==
+[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.
+== 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/bc/1bcz_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=1bcz ConSurf].
+<div style="clear:both"></div>
-'''RECOMBINANT RAT ANNEXIN V, T72S MUTANT'''
+==See Also==
+*[[Annexin 3D structures|Annexin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-Annexin V belongs to a family of eukaryotic calcium-dependent membrane-binding proteins. The calcium-binding sites at the annexin-membrane interface have been investigated in some detail; however, little is known about the functional roles of highly conserved interfacial residues that do not coordinate calcium themselves. In the present study, the importance of tryptophan 185, and threonine or serine at positions 72, 144, 228, and 303, in rat annexin V is investigated by site-directed mutagenesis, X-ray crystallography, and functional assays. The high-resolution crystal structures of the mutants show that the mutations do not cause structural perturbations of the annexin molecule itself or disappearance of bound calcium ions from calcium-binding sites. The assays indicate that relative to wild-type annexin V, loss of the methyl substituent at position 72 (Thr72--&gt;Ser) has no effect while loss of the hydroxyl group (Thr72--&gt;Ala or Thr72--&gt;Lys) causes reduction of membrane binding. Multiple lysine substitutions (e.g., Thr72,Ser144,Ser228,Ser303--&gt;Lys) have a greater adverse effect than the single lysine mutation, suggesting that in annexin V the introduction of potentially favorable electrostatic interactions between the lysine side chains and the net negatively charged membrane surface is not sufficient to overcome the loss of the hydroxyl side chains. Replacement of the unique tryptophan, Trp185, by alanine similarly decreases membrane binding affinity. Taken together, the data suggest that the side chains mutated in this study contribute to phospholipid binding and participate directly in intermolecular contacts with phospholipid membrane components.
+[[Category: Large Structures]]
-==About this Structure==
-BCZ 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=1BCZ OCA].
-==Reference==
-Mutational and crystallographic analyses of interfacial residues in annexin V suggest direct interactions with phospholipid membrane components., Campos B, Mo YD, Mealy TR, Li CW, Swairjo MA, Balch C, Head JF, Retzinger G, Dedman JR, Seaton BA, Biochemistry. 1998 Jun 2;37(22):8004-10. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9609693 9609693]
 [[Category: Rattus norvegicus]]
-[[Category: Single protein]]
+[[Category: Head JF]]
-[[Category: Head, J F.]]
+[[Category: Li CW]]
-[[Category: Li, C W.]]
+[[Category: Mo YD]]
-[[Category: Mo, Y D.]]
+[[Category: Seaton BA]]
-[[Category: Seaton, B A.]]
+[[Category: Swairjo MA]]
-[[Category: Swairjo, M A.]]
-[[Category: CA]]
-[[Category: SO4]]
-[[Category: calcium binding protein]]
-[[Category: phospholipid membrane binding protein]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:09:21 2008''