1sw8

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[[Image:1sw8.gif|left|200px]]
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{{STRUCTURE_1sw8| PDB=1sw8 | SCENE= }}
{{STRUCTURE_1sw8| PDB=1sw8 | SCENE= }}
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'''Solution structure of the N-terminal domain of Human N60D calmodulin refined with paramagnetism based strategy'''
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===Solution structure of the N-terminal domain of Human N60D calmodulin refined with paramagnetism based strategy===
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==Overview==
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The conformational space sampled by the two-domain protein calmodulin has been explored by an approach based on four sets of NMR observables obtained on Tb(3+)- and Tm(3+)-substituted proteins. The observables are the pseudocontact shifts and residual dipolar couplings of the C-terminal domain when lanthanide substitution is at the N-terminal domain. Each set of observables provides independent information on the conformations experienced by the molecule. It is found that not all sterically allowed conformations are equally populated. Taking the N-terminal domain as the reference, the C-terminal domain preferentially resides in a region of space inscribed in a wide elliptical cone. The axis of the cone is tilted by approximately 30 degrees with respect to the direction of the N-terminal part of the interdomain helix, which is known to have a flexible central part in solution. The C-terminal domain also undergoes rotation about the axis defined by the C-terminal part of the interdomain helix. Neither the extended helix conformation initially observed in the solid state for free calcium calmodulin nor the closed conformation(s) adopted by calcium calmodulin either alone or in its adduct(s) with target peptide(s) is among the most preferred ones. These findings are unique, both in terms of structural information obtained on a biomolecule that samples multiple conformations and in terms of the approach developed to achieve the results. The same approach is in principle applicable to other multidomain proteins, as well as to multiple interaction modes between two macromolecular partners.
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(as it appears on PubMed at http://www.pubmed.gov), where 15100408 is the PubMed ID number.
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{{ABSTRACT_PUBMED_15100408}}
==About this Structure==
==About this Structure==
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1SW8 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=1SW8 OCA].
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1SW8 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=1SW8 OCA].
==Reference==
==Reference==
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[[Category: Structural genomic]]
[[Category: Structural genomic]]
[[Category: Structural proteomics in europe]]
[[Category: Structural proteomics in europe]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Apr 13 08:11:24 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 23:07:41 2008''

Revision as of 20:07, 27 July 2008

Image:1sw8.png

Template:STRUCTURE 1sw8

Solution structure of the N-terminal domain of Human N60D calmodulin refined with paramagnetism based strategy

Template:ABSTRACT PUBMED 15100408

About this Structure

1SW8 is a Single protein structure of sequence from Homo sapiens. Full experimental information is available from OCA.

Reference

Experimentally exploring the conformational space sampled by domain reorientation in calmodulin., Bertini I, Del Bianco C, Gelis I, Katsaros N, Luchinat C, Parigi G, Peana M, Provenzani A, Zoroddu MA, Proc Natl Acad Sci U S A. 2004 May 4;101(18):6841-6. Epub 2004 Apr 20. PMID:15100408

Page seeded by OCA on Sun Jul 27 23:07:41 2008

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