1aow

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(New page: 200px<br /><applet load="1aow" size="450" color="white" frame="true" align="right" spinBox="true" caption="1aow, resolution 3.0&Aring;" /> '''ANNEXIN IV'''<br /> ...)
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[[Image:1aow.gif|left|200px]]<br /><applet load="1aow" size="450" color="white" frame="true" align="right" spinBox="true"
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[[Image:1aow.gif|left|200px]]<br /><applet load="1aow" size="350" color="white" frame="true" align="right" spinBox="true"
caption="1aow, resolution 3.0&Aring;" />
caption="1aow, resolution 3.0&Aring;" />
'''ANNEXIN IV'''<br />
'''ANNEXIN IV'''<br />
==Overview==
==Overview==
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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.
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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==
==About this Structure==
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1AOW is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1AOW OCA].
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1AOW is a [http://en.wikipedia.org/wiki/Single_protein 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==
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[[Category: Stoppini, M.]]
[[Category: Stoppini, M.]]
[[Category: Zanotti, G.]]
[[Category: Zanotti, G.]]
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[[Category: 32.5kd calelectrin]]
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[[Category: 32 5kd calelectrin]]
[[Category: calcium/phospholipid-binding protein]]
[[Category: calcium/phospholipid-binding protein]]
[[Category: chromobindin iv]]
[[Category: chromobindin iv]]
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[[Category: protein ii]]
[[Category: protein ii]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Nov 20 11:00:49 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:46:57 2008''

Revision as of 09:46, 21 February 2008


1aow, resolution 3.0Å

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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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