1m9i

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[[Image:1m9i.jpg|left|200px]]
[[Image:1m9i.jpg|left|200px]]
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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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The line below this paragraph, containing "STRUCTURE_1m9i", creates the "Structure Box" on the page.
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|SITE=
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|LIGAND= <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>
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or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
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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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|DOMAIN=
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{{STRUCTURE_1m9i| PDB=1m9i | SCENE= }}
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|RELATEDENTRY=[[1avc|1AVC]]
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1m9i FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1m9i OCA], [http://www.ebi.ac.uk/pdbsum/1m9i PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1m9i RCSB]</span>
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'''Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI'''
'''Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI'''
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[[Category: Freye-Minks, C.]]
[[Category: Freye-Minks, C.]]
[[Category: Kretsinger, R H.]]
[[Category: Kretsinger, R H.]]
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[[Category: annexin]]
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[[Category: Annexin]]
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[[Category: calcium-binding]]
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[[Category: Calcium-binding]]
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[[Category: membrane-binding]]
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[[Category: Membrane-binding]]
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[[Category: mutant t356d]]
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[[Category: Mutant t356d]]
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[[Category: phosphorylation]]
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[[Category: Phosphorylation]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:47:39 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 22:13:09 2008''
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Revision as of 21:47, 2 May 2008

Template:STRUCTURE 1m9i

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 Page seeded by OCA on Sat May 3 00:47:39 2008

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