1aow: Difference between revisions

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[[Image:1aow.gif|left|200px]]


{{Structure
==ANNEXIN IV==
|PDB= 1aow |SIZE=350|CAPTION= <scene name='initialview01'>1aow</scene>, resolution 3.0&Aring;
<StructureSection load='1aow' size='340' side='right'caption='[[1aow]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
|SITE=  
== Structural highlights ==
|LIGAND=  
<table><tr><td colspan='2'>[[1aow]] is a 1 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=1AOW OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1AOW 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]] 3&#8491;</td></tr>
|GENE=  
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1aow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aow OCA], [https://pdbe.org/1aow PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1aow RCSB], [https://www.ebi.ac.uk/pdbsum/1aow PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1aow ProSAT]</span></td></tr>
|DOMAIN=
</table>
|RELATEDENTRY=
== Function ==
|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1aow FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1aow OCA], [http://www.ebi.ac.uk/pdbsum/1aow PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1aow RCSB]</span>
[https://www.uniprot.org/uniprot/ANXA4_BOVIN ANXA4_BOVIN] May play a role in alveolar type II cells through interaction with the surfactant protein SFTPA1 (SP-A).
}}
== 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/ao/1aow_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=1aow ConSurf].
<div style="clear:both"></div>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
The structure of a trigonal crystal form of N-terminally truncated [des-(1-9)] bovine annexin IV, an annexin variant that exhibits the distinctive property of binding both phospholipids and carbohydrates in a Ca2+-dependent manner, has been determined at 3 A (0.3 nm) resolution -space group: R3; cell parameters: a=b=118.560 (8) A and c=82.233 (6) A-. The overall structure of annexin IV, crystallized in the absence of Ca2+ ions, is highly homologous to that of the other known members of the annexin family. The trimeric assembly in the trigonal crystals of annexin IV is quite similar to that found previously in non-isomorphous crystals of human, chicken and rat annexin V and to the subunit arrangement in half of the hexamer of hydra annexin XII. Moreover, it resembles that found in two-dimensional crystals of human annexin V bound to phospholipid monolayers. The propensity of several annexins to generate similar trimeric arrays supports the hypothesis that trimeric complexes of such annexins, including annexin IV, may represent the functional units that interact with membranes.


'''ANNEXIN IV'''
Structure of the trigonal crystal form of bovine annexin IV.,Zanotti G, Malpeli G, Gliubich F, Folli C, Stoppini M, Olivi L, Savoia A, Berni R Biochem J. 1998 Jan 1;329 ( Pt 1):101-6. PMID:9405281<ref>PMID:9405281</ref>


From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 1aow" style="background-color:#fffaf0;"></div>


==Overview==
==See Also==
The structure of a trigonal crystal form of N-terminally truncated [des-(1-9)] bovine annexin IV, an annexin variant that exhibits the distinctive property of binding both phospholipids and carbohydrates in a Ca2+-dependent manner, has been determined at 3 A (0.3 nm) resolution -space group: R3; cell parameters: a=b=118.560 (8) A and c=82.233 (6) A-. The overall structure of annexin IV, crystallized in the absence of Ca2+ ions, is highly homologous to that of the other known members of the annexin family. The trimeric assembly in the trigonal crystals of annexin IV is quite similar to that found previously in non-isomorphous crystals of human, chicken and rat annexin V and to the subunit arrangement in half of the hexamer of hydra annexin XII. Moreover, it resembles that found in two-dimensional crystals of human annexin V bound to phospholipid monolayers. The propensity of several annexins to generate similar trimeric arrays supports the hypothesis that trimeric complexes of such annexins, including annexin IV, may represent the functional units that interact with membranes.
*[[Annexin 3D structures|Annexin 3D structures]]
 
== References ==
==About this Structure==
<references/>
1AOW is a [[Single protein]] structure of sequence 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=1AOW OCA].
__TOC__
 
</StructureSection>
==Reference==
Structure of the trigonal crystal form of bovine annexin IV., Zanotti G, Malpeli G, Gliubich F, Folli C, Stoppini M, Olivi L, Savoia A, Berni R, Biochem J. 1998 Jan 1;329 ( Pt 1):101-6. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/9405281 9405281]
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Single protein]]
[[Category: Large Structures]]
[[Category: Berni, R.]]
[[Category: Berni R]]
[[Category: Folli, C.]]
[[Category: Folli C]]
[[Category: Gliubich, F.]]
[[Category: Gliubich F]]
[[Category: Malpeli, G.]]
[[Category: Malpeli G]]
[[Category: Olivi, L.]]
[[Category: Olivi L]]
[[Category: Savoia, A.]]
[[Category: Savoia A]]
[[Category: Stoppini, M.]]
[[Category: Stoppini M]]
[[Category: Zanotti, G.]]
[[Category: Zanotti G]]
[[Category: 32 5kd calelectrin]]
[[Category: calcium/phospholipid-binding protein]]
[[Category: chromobindin iv]]
[[Category: endonexin i]]
[[Category: lipocortin iv]]
[[Category: protein ii]]
 
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