1aow: Difference between revisions

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==ANNEXIN IV==
==ANNEXIN IV==
<StructureSection load='1aow' size='340' side='right' caption='[[1aow]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
<StructureSection load='1aow' size='340' side='right'caption='[[1aow]], [[Resolution|resolution]] 3.00&Aring;' scene=''>
== Structural highlights ==
== Structural highlights ==
<table><tr><td colspan='2'>[[1aow]] is a 1 chain structure with 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]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1AOW FirstGlance]. <br>
<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>
</td></tr><tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><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://pdbe.org/1aow PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1aow RCSB], [http://www.ebi.ac.uk/pdbsum/1aow PDBsum]</span></td></tr>
</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>
<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>
</table>
</table>
== Function ==
== Function ==
[[http://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).  
[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 ==
== Evolutionary Conservation ==
[[Image:Consurf_key_small.gif|200px|right]]
[[Image:Consurf_key_small.gif|200px|right]]
Check<jmol>
Check<jmol>
   <jmolCheckbox>
   <jmolCheckbox>
     <scriptWhenChecked>select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/ao/1aow_consurf.spt"</scriptWhenChecked>
     <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>
     <scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
     <text>to colour the structure by Evolutionary Conservation</text>
     <text>to colour the structure by Evolutionary Conservation</text>
   </jmolCheckbox>
   </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/chain_selection.php?pdb_ID=2ata ConSurf].
</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="clear:both"></div>
<div style="background-color:#fffaf0;">
<div style="background-color:#fffaf0;">
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==See Also==
==See Also==
*[[Annexin|Annexin]]
*[[Annexin 3D structures|Annexin 3D structures]]
== References ==
== References ==
<references/>
<references/>
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</StructureSection>
</StructureSection>
[[Category: Bos taurus]]
[[Category: Bos taurus]]
[[Category: Berni, R]]
[[Category: Large Structures]]
[[Category: Folli, C]]
[[Category: Berni R]]
[[Category: Gliubich, F]]
[[Category: Folli C]]
[[Category: Malpeli, G]]
[[Category: Gliubich F]]
[[Category: Olivi, L]]
[[Category: Malpeli G]]
[[Category: Savoia, A]]
[[Category: Olivi L]]
[[Category: Stoppini, M]]
[[Category: Savoia A]]
[[Category: Zanotti, G]]
[[Category: Stoppini M]]
[[Category: 32 5kd calelectrin]]
[[Category: Zanotti G]]
[[Category: Calcium-phospholipid-binding protein complex]]
[[Category: Calcium/phospholipid-binding protein]]
[[Category: Chromobindin iv]]
[[Category: Endonexin i]]
[[Category: Lipocortin iv]]
[[Category: Protein ii]]

Latest revision as of 13:54, 2 August 2023

ANNEXIN IVANNEXIN IV

Structural highlights

1aow is a 1 chain structure with sequence from Bos taurus. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:X-ray diffraction, Resolution 3Å
Resources:FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

ANXA4_BOVIN May play a role in alveolar type II cells through interaction with the surfactant protein SFTPA1 (SP-A).

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

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.

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[1]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

See Also

References

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

1aow, resolution 3.00Å

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