1aow: Difference between revisions
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<StructureSection load='1aow' size='340' side='right'caption='[[1aow]], [[Resolution|resolution]] 3.00Å' scene=''> | <StructureSection load='1aow' size='340' side='right'caption='[[1aow]], [[Resolution|resolution]] 3.00Å' scene=''> | ||
== Structural highlights == | == Structural highlights == | ||
<table><tr><td colspan='2'>[[1aow]] is a 1 chain structure with sequence from [ | <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'>[ | </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 == | ||
[[ | [[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]] | ||
Revision as of 13:22, 17 February 2021
ANNEXIN IVANNEXIN IV
Structural highlights
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 PubMedThe 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 AlsoReferences |
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