1aow
From Proteopedia
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| - | [[Image:1aow.gif|left|200px]] | + | [[Image:1aow.gif|left|200px]] |
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| - | '''ANNEXIN IV''' | + | {{Structure |
| + | |PDB= 1aow |SIZE=350|CAPTION= <scene name='initialview01'>1aow</scene>, resolution 3.0Å | ||
| + | |SITE= | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''ANNEXIN IV''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1AOW is a [ | + | 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]. |
==Reference== | ==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:// | + | 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: Single protein]] | ||
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[[Category: protein ii]] | [[Category: protein ii]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:00:29 2008'' |
Revision as of 08:00, 20 March 2008
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
ANNEXIN IV
Overview
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.
About this Structure
1AOW is a Single protein structure of sequence from Bos taurus. Full crystallographic information is available from OCA.
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:9405281
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