2hf5
From Proteopedia
| Line 1: | Line 1: | ||
[[Image:2hf5.jpg|left|200px]] | [[Image:2hf5.jpg|left|200px]] | ||
| - | + | <!-- | |
| - | + | The line below this paragraph, containing "STRUCTURE_2hf5", creates the "Structure Box" on the page. | |
| - | + | You may change the PDB parameter (which sets the PDB file loaded into the applet) | |
| - | + | or the SCENE parameter (which sets the initial scene displayed when the page is loaded), | |
| - | + | or leave the SCENE parameter empty for the default display. | |
| - | + | --> | |
| - | + | {{STRUCTURE_2hf5| PDB=2hf5 | SCENE= }} | |
| - | + | ||
| - | + | ||
| - | }} | + | |
'''The structure and function of a novel two-site calcium-binding fragment of calmodulin''' | '''The structure and function of a novel two-site calcium-binding fragment of calmodulin''' | ||
| Line 29: | Line 26: | ||
[[Category: McIntosh, L P.]] | [[Category: McIntosh, L P.]] | ||
[[Category: Reid, R E.]] | [[Category: Reid, R E.]] | ||
| - | [[Category: | + | [[Category: Calcium-binding]] |
| - | [[Category: | + | [[Category: Calmodulin]] |
| - | [[Category: | + | [[Category: Calmodulin fragment]] |
| - | [[Category: | + | [[Category: Ef-hand]] |
| - | [[Category: | + | [[Category: Hlh]] |
| - | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun May 4 06:13:08 2008'' | |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | |
Revision as of 03:13, 4 May 2008
The structure and function of a novel two-site calcium-binding fragment of calmodulin
Overview
Calmodulin (CaM) is an EF-hand protein composed of two calcium (Ca(2+))-binding EF-hand motifs in its N-domain (EF-1 and EF-2) and two in its C-domain (EF-3 and EF-4). In this study, we examined the structure, dynamics, and Ca(2+)-binding properties of a fragment of CaM containing only EF-2 and EF-3 and the intervening linker sequence (CaM2/3). Based on NMR spectroscopic analyses, Ca(2+)-free CaM2/3 is predominantly unfolded, but upon binding Ca(2+), adopts a monomeric structure composed of two EF-hand motifs bridged by a short antiparallel beta-sheet. Despite having an "even-odd" pairing of EF-hands, the tertiary structure of CaM2/3 is similar to both the "odd-even" paired N- and C-domains of Ca(2+)-ligated CaM, with the conformationally flexible linker sequence adopting the role of an inter-EF-hand loop. However, unlike either CaM domain, CaM2/3 exhibits stepwise Ca(2+) binding with a K (d1) = 30 +/- 5 microM to EF-3, and a K (d2) > 1000 microM to EF-2. Binding of the first equivalent of Ca(2+) induces the cooperative folding of CaM2/3. In the case of native CaM, stacking interactions between four conserved aromatic residues help to hold the first and fourth helices of each EF-hand domain together, while the loop between EF-hands covalently tethers the second and third helices. In contrast, these aromatic residues lie along the second and third helices of CaM2/3, and thus are positioned adjacent to the loop between its "even-odd" paired EF-hands. This nonnative hydrophobic core packing may contribute to the weak Ca(2+) affinity exhibited by EF-2 in the context of CaM2/3.
About this Structure
2HF5 is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
Reference
Calcium-induced folding of a fragment of calmodulin composed of EF-hands 2 and 3., Lakowski TM, Lee GM, Okon M, Reid RE, McIntosh LP, Protein Sci. 2007 Jun;16(6):1119-32. Epub 2007 May 1. PMID:17473011 Page seeded by OCA on Sun May 4 06:13:08 2008
