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| - | [[Image:1zfo.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1zfo| PDB=1zfo | SCENE= }} | | {{STRUCTURE_1zfo| PDB=1zfo | SCENE= }} |
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| - | '''AMINO-TERMINAL LIM-DOMAIN PEPTIDE OF LASP-1, NMR'''
| + | ===AMINO-TERMINAL LIM-DOMAIN PEPTIDE OF LASP-1, NMR=== |
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| - | ==Overview==
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| - | The three-dimensional solution structure of the 1:1 complex between the synthetic peptide ZF-1 and zinc was determined by 1H NMR spectroscopy. The peptide, initially isolated from pig intestines, is identical in sequence to the 30 N-terminal amino acid residues of the human protein Lasp-1 belonging to the LIM domain protein family. The final set of 20 energy-refined NMR conformers has an average rmsd relative to the mean structure of 0.55 A for the backbone atoms of residues 3-30. Calculations without zinc atom constraints unambiguously identified Cys 5, Cys 8, His 26, and Cys 29 as the zinc-coordinating residues. LIM domains consist of two sequential zinc-binding modules and the NMR structure of the ZF-1-zinc complex is the first example of a structure of an isolated module. Comparison with the known structures of the N-terminal zinc-binding modules of both the second LIM domain of chicken CRP and rat CRIP with which ZF-1 shares 50% and 43% sequence identity, respectively, supports the notion that the zinc-binding modules of the LIM domain have a conserved structural motif and identifies local regions of structural diversity. The similarities include conserved zinc-coordinating residues, a rubredoxin knuckle involving Cys 5 and Cys 8, and the coordination of the zinc ion by histidine N delta in contrast to the more usual coordination by N epsilon observed for other zinc-finger domains. The present structure determination of the ZF-1-zinc complex establishes the N-terminal half of a LIM domain as an independent folding unit. The structural similarities of N- and C-terminal zinc-binding modules of the LIM domains, despite limited sequence identity, lead to the proposal of a single zinc-binding motif in LIM domains. The coordinates are available from the Brookhaven protein data bank, entry 1ZFO.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_8841116}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 8841116 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_8841116}} |
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| | ==About this Structure== | | ==About this Structure== |
| - | 1ZFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZFO OCA]. | + | 1ZFO is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Sus_scrofa Sus scrofa]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZFO OCA]. |
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| | ==Reference== | | ==Reference== |
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| | [[Category: Metal-binding protein]] | | [[Category: Metal-binding protein]] |
| | [[Category: Zinc-finger]] | | [[Category: Zinc-finger]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 17:34:01 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jul 28 11:09:57 2008'' |
Revision as of 08:10, 28 July 2008
Template:STRUCTURE 1zfo
AMINO-TERMINAL LIM-DOMAIN PEPTIDE OF LASP-1, NMR
Template:ABSTRACT PUBMED 8841116
About this Structure
1ZFO is a Single protein structure of sequence from Sus scrofa. Full experimental information is available from OCA.
Reference
Solution structure of a naturally-occurring zinc-peptide complex demonstrates that the N-terminal zinc-binding module of the Lasp-1 LIM domain is an independent folding unit., Hammarstrom A, Berndt KD, Sillard R, Adermann K, Otting G, Biochemistry. 1996 Oct 1;35(39):12723-32. PMID:8841116
Page seeded by OCA on Mon Jul 28 11:09:57 2008
