1m9i

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[[Image:1m9i.jpg|left|200px]]<br /><applet load="1m9i" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1m9i.jpg|left|200px]]
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caption="1m9i, resolution 2.65&Aring;" />
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'''Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI'''<br />
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{{Structure
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|PDB= 1m9i |SIZE=350|CAPTION= <scene name='initialview01'>1m9i</scene>, resolution 2.65&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM ION'>CA</scene>
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|ACTIVITY=
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|GENE= ANX6 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
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}}
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'''Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1M9I is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M9I OCA].
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1M9I is a [[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=1M9I OCA].
==Reference==
==Reference==
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Structural and dynamic changes in human annexin VI induced by a phosphorylation-mimicking mutation, T356D., Freye-Minks C, Kretsinger RH, Creutz CE, Biochemistry. 2003 Jan 28;42(3):620-30. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=12534274 12534274]
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Structural and dynamic changes in human annexin VI induced by a phosphorylation-mimicking mutation, T356D., Freye-Minks C, Kretsinger RH, Creutz CE, Biochemistry. 2003 Jan 28;42(3):620-30. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/12534274 12534274]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: phosphorylation]]
[[Category: phosphorylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:52:56 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:40:41 2008''

Revision as of 10:40, 20 March 2008


PDB ID 1m9i

Drag the structure with the mouse to rotate
, resolution 2.65Å
Ligands:
Gene: ANX6 (Homo sapiens)
Coordinates: save as pdb, mmCIF, xml



Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI


Overview

Phosphorylation of some members of the annexin family of proteins may play a significant role in controlling their calcium-dependent interactions with membranes. Recent electron microscopic studies of annexin VI revealed that the protein's two core domains exhibit a great degree of flexibility and are able to undergo a relative conformational change that could potentially initiate contacts between membranes [Avila-Sakar, A. J., et al. (2000) J. Struct. Biol. 130, 54-62]. To assess the possibility of a regulatory role of phosphorylation in this behavior, the crystal structure of a phosphorylation-mimicking mutant (T356D in the flexible connector region of human annexin VI) was determined to 2.65 A resolution. When the mutant is compared to the wild-type annexin VI, subtle differences are seen at the site of the mutation, while larger changes are evident in one of the calcium-binding loops and in the presence of five calcium ions. Furthermore, biochemical studies provide evidence for additional conformational differences between the T356D and wild-type solution structures. Fluorescence emission and acrylamide quenching suggest a higher level of solvent exposure of Trp-343 in the connector region of T356D in the presence of calcium. Comparisons of retardation coefficients in native gel electrophoresis reveal that T356D has a more extended shape, while proteolytic studies show a greater accessibility of a trypsin cleavage site inside the linker region, indicating a conformation more open than the wild-type form. These data provide insights into a possible regulatory mechanism leading to a higher degree of flexibility and possibly a higher calcium binding affinity of annexin VI upon phosphorylation.

About this Structure

1M9I is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Structural and dynamic changes in human annexin VI induced by a phosphorylation-mimicking mutation, T356D., Freye-Minks C, Kretsinger RH, Creutz CE, Biochemistry. 2003 Jan 28;42(3):620-30. PMID:12534274

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