1ain: Difference between revisions

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-[[Image:1ain.gif|left|200px]]
- {{Structure
+==CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS RESOLUTION==
-|PDB= 1ain |SIZE=350|CAPTION= <scene name='initialview01'>1ain</scene>, resolution 2.5&Aring;
+<StructureSection load='1ain' size='340' side='right'caption='[[1ain]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
-|SITE=
+== Structural highlights ==
-|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
+<table><tr><td colspan='2'>[[1ain]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AIN 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]] 2.5&#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></td></tr>
-|DOMAIN=
+<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1ain FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ain OCA], [https://pdbe.org/1ain PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1ain RCSB], [https://www.ebi.ac.uk/pdbsum/1ain PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1ain ProSAT]</span></td></tr>
-|RELATEDENTRY=
+</table>
-|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ain FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1ain OCA], [http://www.ebi.ac.uk/pdbsum/1ain PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1ain RCSB]</span>
+== Function ==
-}}
+[https://www.uniprot.org/uniprot/ANXA1_HUMAN ANXA1_HUMAN] Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.
+== 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/ai/1ain_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=1ain ConSurf].
+<div style="clear:both"></div>
-'''CRYSTAL STRUCTURE OF HUMAN ANNEXIN I AT 2.5 ANGSTROMS RESOLUTION'''
+==See Also==
+*[[Annexin 3D structures|Annexin 3D structures]]
+__TOC__
-==Overview==
+</StructureSection>
-cDNA coding for N-terminally truncated human annexin I, a member of the family of Ca(2+)-dependent phospholipid binding proteins, has been cloned and expressed in Escherichia coli. The expressed protein is biologically active, and has been purified and crystallized in space group P2(1)2(1)2(1) with cell dimensions a = 139.36 A, b = 67.50 A, and c = 42.11 A. The crystal structure has been determined by molecular replacement at 3.0 A resolution using the annexin V core structure as the search model. The average backbone deviation between these two structures is 2.34 A. The structure has been refined to an R-factor of 17.7% at 2.5 A resolution. Six calcium sites have been identified in the annexin I structure. Each is located in the loop region of the helix-loop-helix motif. Two of the six calcium sites in annexin I are not occupied in the annexin V structure. The superpositions of the corresponding loop regions in the four domains show that the calcium binding loops in annexin I can be divided into two classes: type II and type III. Both classes are different from the well-known EF-hand motif (type I).
-==About this Structure==
-AIN is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1AIN OCA].
-==Reference==
-Crystal structure of human annexin I at 2.5 A resolution., Weng X, Luecke H, Song IS, Kang DS, Kim SH, Huber R, Protein Sci. 1993 Mar;2(3):448-58. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8453382 8453382]
 [[Category: Homo sapiens]]
-[[Category: Single protein]]
+[[Category: Large Structures]]
-[[Category: Kim, S H.]]
+[[Category: Kim S-H]]
-[[Category: calcium/phospholipid binding]]
-''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 18:41:03 2008''