1zfo: Difference between revisions
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[[Image:1zfo.gif|left|200px]]< | [[Image:1zfo.gif|left|200px]] | ||
'''AMINO-TERMINAL LIM-DOMAIN PEPTIDE OF LASP-1, NMR''' | {{Structure | ||
|PDB= 1zfo |SIZE=350|CAPTION= <scene name='initialview01'>1zfo</scene> | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene> and <scene name='pdbligand=ACE:ACETYL GROUP'>ACE</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''AMINO-TERMINAL LIM-DOMAIN PEPTIDE OF LASP-1, NMR''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1ZFO is a [ | 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]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/8841116 8841116] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
[[Category: Sus scrofa]] | [[Category: Sus scrofa]] | ||
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[[Category: zinc-finger]] | [[Category: zinc-finger]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:34:54 2008'' | ||
Revision as of 13:34, 20 March 2008
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| Ligands: | ZN and ACE | ||||||||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||||||||
AMINO-TERMINAL LIM-DOMAIN PEPTIDE OF LASP-1, NMR
Overview
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.
About this Structure
1ZFO is a Single protein structure of sequence from Sus scrofa. Full crystallographic 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
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