From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1m9i.jpg|left|200px]] | + | {{Seed}} |
| | + | [[Image:1m9i.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1m9i| PDB=1m9i | SCENE= }} | | {{STRUCTURE_1m9i| PDB=1m9i | SCENE= }} |
| | | | |
| - | '''Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI'''
| + | ===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.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_12534274}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 12534274 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_12534274}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Mutant t356d]] | | [[Category: Mutant t356d]] |
| | [[Category: Phosphorylation]] | | [[Category: Phosphorylation]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 00:47:39 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Wed Jul 2 23:29:49 2008'' |
Revision as of 20:29, 2 July 2008
Template:STRUCTURE 1m9i
Crystal Structure Of Phosphorylation-Mimicking Mutant T356D Of Annexin VI
Template:ABSTRACT PUBMED 12534274
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 Wed Jul 2 23:29:49 2008
