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1qzp

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[[Image:1qzp.jpg|left|200px]]
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'''NMR structure of the human dematin headpiece domain'''<br />
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{{Structure
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|PDB= 1qzp |SIZE=350|CAPTION= <scene name='initialview01'>1qzp</scene>
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|SITE=
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|LIGAND=
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'''NMR structure of the human dematin headpiece domain'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1QZP is a [http://en.wikipedia.org/wiki/Single_protein 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=1QZP OCA].
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1QZP 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=1QZP OCA].
==Reference==
==Reference==
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The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site., Frank BS, Vardar D, Chishti AH, McKnight CJ, J Biol Chem. 2004 Feb 27;279(9):7909-16. Epub 2003 Dec 2. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14660664 14660664]
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The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site., Frank BS, Vardar D, Chishti AH, McKnight CJ, J Biol Chem. 2004 Feb 27;279(9):7909-16. Epub 2003 Dec 2. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14660664 14660664]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: villin headpiece]]
[[Category: villin headpiece]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:45:31 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:44:53 2008''

Revision as of 11:44, 20 March 2008


PDB ID 1qzp

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NMR structure of the human dematin headpiece domain


Contents

Overview

Dematin (band 4.9) is found in the junctional complex of the spectrin cytoskeleton that supports the erythrocyte cell membrane. Dematin is a member of the larger class of cytoskeleton-associated proteins that contain a modular "headpiece" domain at their extreme C termini. The dematin headpiece domain provides the second F-actin-binding site required for in vitro F-actin bundling. The dematin headpiece is found in two forms in the cell, one of 68 residues (DHP) and one containing a 22-amino acid insert near its N terminus (DHP+22). In addition, dematin contains the only headpiece domain that is phosphorylated, in vivo. The 22-amino acid insert in DHP+22 appeared unstructured in NMR spectra; therefore, we have determined the three-dimensional structure of DHP by multidimensional NMR methods. Although the overall three-dimensional structure of DHP is similar to that of the villin headpiece, there are two novel characteristics revealed by this structure. First, unlike villin headpiece that contains a single buried salt bridge, DHP contains a buried charged cluster comprising residues Glu(39), Arg(66), Lys(70), and the C-terminal carboxylate of Phe(76). Second, (15)N relaxation experiments indicate that the longer "variable loop" region near the N terminus of DHP (residues 20-29) is dynamic, undergoing significantly greater motions that the rest of the structure. Furthermore, NMR chemical shift changes indicate that the conformation of the dynamic variable loop is altered by phosphorylation of serine 74, which is far in the sequence from the variable loop region. Our results suggest that phosphorylation of the dematin headpiece acts as a conformational switch within this headpiece domain.

Disease

Known diseases associated with this structure: Amyotrophic lateral sclerosis, CHMP2B-related OMIM:[609512], Dementia, familial, nonspecific OMIM:[609512], XY sex reversal OMIM:[602424]

About this Structure

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

Reference

The NMR structure of dematin headpiece reveals a dynamic loop that is conformationally altered upon phosphorylation at a distal site., Frank BS, Vardar D, Chishti AH, McKnight CJ, J Biol Chem. 2004 Feb 27;279(9):7909-16. Epub 2003 Dec 2. PMID:14660664

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