From Proteopedia
(Difference between revisions)
proteopedia linkproteopedia link
|
|
| Line 1: |
Line 1: |
| - | [[Image:1u5p.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1u5p.png|left|200px]] |
| | | | |
| | <!-- | | <!-- |
| Line 9: |
Line 10: |
| | {{STRUCTURE_1u5p| PDB=1u5p | SCENE= }} | | {{STRUCTURE_1u5p| PDB=1u5p | SCENE= }} |
| | | | |
| - | '''Crystal Structure of Repeats 15 and 16 of Chicken Brain Alpha Spectrin'''
| + | ===Crystal Structure of Repeats 15 and 16 of Chicken Brain Alpha Spectrin=== |
| | | | |
| | | | |
| - | ==Overview==
| + | <!-- |
| - | Previous X-ray crystal structures have shown that linkers of five amino acid residues connecting pairs of chicken brain alpha-spectrin and human erythroid beta-spectrin repeats can undergo bending without losing their alpha-helical structure. To test whether bending at one linker can influence bending at an adjacent linker, the structures of two and three repeat fragments of chicken brain alpha-spectrin have been determined by X-ray crystallography. The structure of the three-repeat fragment clearly shows that bending at one linker can occur independently of bending at an adjacent linker. This observation increases the possible trajectories of modeled chains of spectrin repeats. Furthermore, the three-repeat molecule crystallized as an antiparallel dimer with a significantly smaller buried interfacial area than that of alpha-actinin, a spectrin-related molecule, but large enough and of a type indicating biological specificity. Comparison of the structures of the spectrin and alpha-actinin dimers supports weak association of the former, which could not be detected by analytical ultracentrifugation, versus strong association of the latter, which has been observed by others. To correlate features of the structure with solution properties and to test a previous model of stable spectrin and dystrophin repeats, the number of inter-helical interactions in each repeat of several spectrin structures were counted and compared to their thermal stabilities. Inter-helical interactions, but not all interactions, increased in parallel with measured thermal stabilities of each repeat and in agreement with the thermal stabilities of two and three repeats and also partial repeats of spectrin.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_15522301}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 15522301 is the PubMed ID number. |
| | + | --> |
| | + | {{ABSTRACT_PUBMED_15522301}} |
| | | | |
| | ==About this Structure== | | ==About this Structure== |
| Line 30: |
Line 34: |
| | [[Category: Alpha-helical linker region]] | | [[Category: Alpha-helical linker region]] |
| | [[Category: Two repeats of spectrin]] | | [[Category: Two repeats of spectrin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 10:47:11 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 16:59:19 2008'' |
Revision as of 13:59, 28 July 2008
Template:STRUCTURE 1u5p
Crystal Structure of Repeats 15 and 16 of Chicken Brain Alpha Spectrin
Template:ABSTRACT PUBMED 15522301
About this Structure
1U5P is a Single protein structure of sequence from Gallus gallus. Full crystallographic information is available from OCA.
Reference
Independent movement, dimerization and stability of tandem repeats of chicken brain alpha-spectrin., Kusunoki H, Minasov G, Macdonald RI, Mondragon A, J Mol Biol. 2004 Nov 19;344(2):495-511. PMID:15522301
Page seeded by OCA on Mon Jul 28 16:59:19 2008
