2hf5: Difference between revisions

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[[Image:2hf5.jpg|left|200px]]
{{Seed}}
[[Image:2hf5.png|left|200px]]


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{{STRUCTURE_2hf5|  PDB=2hf5  |  SCENE=  }}  
{{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===




==Overview==
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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) &gt; 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.
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==About this Structure==
==About this Structure==
2HF5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HF5 OCA].  
2HF5 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2HF5 OCA].  


==Reference==
==Reference==
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[[Category: Ef-hand]]
[[Category: Ef-hand]]
[[Category: Hlh]]
[[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 Tue Jul 29 16:35:24 2008''

Revision as of 13:35, 29 July 2008

File:2hf5.png

Template:STRUCTURE 2hf5

The structure and function of a novel two-site calcium-binding fragment of calmodulin

Template:ABSTRACT PUBMED 17473011

About this Structure

2HF5 is a Single protein structure of sequence from Homo sapiens. Full experimental 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

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