1znf: Difference between revisions

No edit summary
No edit summary
 
(12 intermediate revisions by the same user not shown)
Line 1: Line 1:
[[Image:1znf.gif|left|200px]]


<!--
==THREE-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER DNA-BINDING DOMAIN==
The line below this paragraph, containing "STRUCTURE_1znf", creates the "Structure Box" on the page.
<StructureSection load='1znf' size='340' side='right'caption='[[1znf]]' scene=''>
You may change the PDB parameter (which sets the PDB file loaded into the applet)
== Structural highlights ==
or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
<table><tr><td colspan='2'>[[1znf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The March 2007 RCSB PDB [https://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/index.html Molecule of the Month] feature on ''Zinc Fingers''  by David S. Goodsell is [https://dx.doi.org/10.2210/rcsb_pdb/mom_2007_3 10.2210/rcsb_pdb/mom_2007_3]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ZNF FirstGlance]. <br>
or leave the SCENE parameter empty for the default display.
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR, 37 models</td></tr>
-->
<tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene>, <scene name='pdbligand=NH2:AMINO+GROUP'>NH2</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
{{STRUCTURE_1znf| PDB=1znf  |  SCENE= }}
<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1znf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1znf OCA], [https://pdbe.org/1znf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1znf RCSB], [https://www.ebi.ac.uk/pdbsum/1znf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1znf ProSAT]</span></td></tr>
 
</table>
'''THREE-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER DNA-BINDING DOMAIN'''
== Function ==
 
[https://www.uniprot.org/uniprot/XFIN_XENLA XFIN_XENLA] Binds to poly-G sequences in RNA. May function in post-translational regulation processes.
 
<div style="background-color:#fffaf0;">
==Overview==
== Publication Abstract from PubMed ==
The three-dimensional solution structure of a zinc finger nucleic acid binding motif has been determined by nuclear magnetic resonance (NMR) spectroscopy. Spectra of a synthetic peptide corresponding to a single zinc finger from the Xenopus protein Xfin yielded distance and dihedral angle constraints that were used to generate structures from distance geometry and restrained molecular dynamics calculations. The zinc finger is an independently folded domain with a compact globular structure in which the zinc atom is bound by two cysteine and two histidine ligands. The polypeptide backbone fold consists of a well-defined helix, starting as alpha and ending as 3(10) helix, packed against two beta strands that are arranged in a hairpin structure. A high density of basic and polar amino acid side chains on the exposed face of the helix are probably involved in DNA binding.
The three-dimensional solution structure of a zinc finger nucleic acid binding motif has been determined by nuclear magnetic resonance (NMR) spectroscopy. Spectra of a synthetic peptide corresponding to a single zinc finger from the Xenopus protein Xfin yielded distance and dihedral angle constraints that were used to generate structures from distance geometry and restrained molecular dynamics calculations. The zinc finger is an independently folded domain with a compact globular structure in which the zinc atom is bound by two cysteine and two histidine ligands. The polypeptide backbone fold consists of a well-defined helix, starting as alpha and ending as 3(10) helix, packed against two beta strands that are arranged in a hairpin structure. A high density of basic and polar amino acid side chains on the exposed face of the helix are probably involved in DNA binding.


==About this Structure==
Three-dimensional solution structure of a single zinc finger DNA-binding domain.,Lee MS, Gippert GP, Soman KV, Case DA, Wright PE Science. 1989 Aug 11;245(4918):635-7. PMID:2503871<ref>PMID:2503871</ref>
1ZNF is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Xenopus_laevis Xenopus laevis]. The following page contains interesting information on the relation of 1ZNF with [[http://pdb.rcsb.org/pdb/static.do?p=education_discussion/molecule_of_the_month/pdb87_1.html Zinc Fingers]]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZNF OCA].


==Reference==
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
Three-dimensional solution structure of a single zinc finger DNA-binding domain., Lee MS, Gippert GP, Soman KV, Case DA, Wright PE, Science. 1989 Aug 11;245(4918):635-7. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/2503871 2503871]
</div>
[[Category: Single protein]]
<div class="pdbe-citations 1znf" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: RCSB PDB Molecule of the Month]]
[[Category: Xenopus laevis]]
[[Category: Xenopus laevis]]
[[Category: Zinc Fingers]]
[[Category: Zinc Fingers]]
[[Category: Case, D A.]]
[[Category: Case DA]]
[[Category: Gippert, G P.]]
[[Category: Gippert GP]]
[[Category: Lee, M S.]]
[[Category: Lee MS]]
[[Category: Soman, K V.]]
[[Category: Soman KV]]
[[Category: Wright, P E.]]
[[Category: Wright PE]]
[[Category: Zinc finger dna binding domain]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May  3 17:50:38 2008''

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

OCA