1w45

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(New page: 200px<br /> <applet load="1w45" size="450" color="white" frame="true" align="right" spinBox="true" caption="1w45, resolution 2.51&Aring;" /> '''THE 2.5 ANGSTROEM S...)
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caption="1w45, resolution 2.51&Aring;" />
caption="1w45, resolution 2.51&Aring;" />
'''THE 2.5 ANGSTROEM STRUCTURE OF THE K16A MUTANT OF ANNEXIN A8, WHICH HAS AN INTACT N-TERMINUS.'''<br />
'''THE 2.5 ANGSTROEM STRUCTURE OF THE K16A MUTANT OF ANNEXIN A8, WHICH HAS AN INTACT N-TERMINUS.'''<br />
==Overview==
==Overview==
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Annexin A8 is a relatively infrequent and poorly studied member of this, large family of calcium-binding and membrane-binding proteins. It is, however, associated with a specific disease, acute promyelocytic leukemia., We have solved its three-dimensional structure, which includes a, moderately long and intact N terminus. The structure is closest to that of, annexin A3 and highlights several important regions of inherent, flexibility in the annexin molecule. The N terminus resembles that of, annexin A3, as it lies along the concave surface of the molecule and, inserts partially into the hydrophilic channel in its centre. Since both, annexins A3 and A8 are expressed in promyelocytic cells during their, differentiation, the similarity in their structures might suggest a, functional relationship.
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Annexin A8 is a relatively infrequent and poorly studied member of this large family of calcium-binding and membrane-binding proteins. It is, however, associated with a specific disease, acute promyelocytic leukemia. We have solved its three-dimensional structure, which includes a moderately long and intact N terminus. The structure is closest to that of annexin A3 and highlights several important regions of inherent flexibility in the annexin molecule. The N terminus resembles that of annexin A3, as it lies along the concave surface of the molecule and inserts partially into the hydrophilic channel in its centre. Since both annexins A3 and A8 are expressed in promyelocytic cells during their differentiation, the similarity in their structures might suggest a functional relationship.
==About this Structure==
==About this Structure==
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1W45 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1W45 OCA].
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1W45 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1W45 OCA].
==Reference==
==Reference==
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[[Category: Rety, S.]]
[[Category: Rety, S.]]
[[Category: Russo-Marie, F.]]
[[Category: Russo-Marie, F.]]
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[[Category: Santos, J.Sopkova-De.Oliveira.]]
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[[Category: Santos, J Sopkova-De Oliveira.]]
[[Category: annexin family]]
[[Category: annexin family]]
[[Category: calcium and phospholipid binding proteins]]
[[Category: calcium and phospholipid binding proteins]]
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[[Category: intact n-terminus]]
[[Category: intact n-terminus]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 19:46:33 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 15:40:17 2008''

Revision as of 13:40, 21 February 2008


1w45, resolution 2.51Å

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THE 2.5 ANGSTROEM STRUCTURE OF THE K16A MUTANT OF ANNEXIN A8, WHICH HAS AN INTACT N-TERMINUS.

Overview

Annexin A8 is a relatively infrequent and poorly studied member of this large family of calcium-binding and membrane-binding proteins. It is, however, associated with a specific disease, acute promyelocytic leukemia. We have solved its three-dimensional structure, which includes a moderately long and intact N terminus. The structure is closest to that of annexin A3 and highlights several important regions of inherent flexibility in the annexin molecule. The N terminus resembles that of annexin A3, as it lies along the concave surface of the molecule and inserts partially into the hydrophilic channel in its centre. Since both annexins A3 and A8 are expressed in promyelocytic cells during their differentiation, the similarity in their structures might suggest a functional relationship.

About this Structure

1W45 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

The crystal structure of annexin A8 is similar to that of annexin A3., Rety S, Sopkova-de Oliveira Santos J, Dreyfuss L, Blondeau K, Hofbauerova K, Raguenes-Nicol C, Kerboeuf D, Renouard M, Russo-Marie F, Lewit-Bentley A, J Mol Biol. 2005 Feb 4;345(5):1131-9. Epub 2004 Dec 8. PMID:15644210

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