1m9i: Difference between revisions
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{{STRUCTURE_1m9i| PDB=1m9i | SCENE= }} | |||
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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.]] | ||
[[Category: | [[Category: Annexin]] | ||
[[Category: | [[Category: Calcium-binding]] | ||
[[Category: | [[Category: Membrane-binding]] | ||
[[Category: | [[Category: Mutant t356d]] | ||
[[Category: | [[Category: Phosphorylation]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:47:39 2008'' | |||
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Revision as of 21:47, 2 May 2008
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
