View source for 1znf


==THREE-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER DNA-BINDING DOMAIN==
<StructureSection load='1znf' size='340' side='right'caption='[[1znf]]' scene=''>
== Structural highlights ==
<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>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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>
<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>
== 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;">
== 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.

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>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<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: Zinc Fingers]]
[[Category: Case DA]]
[[Category: Gippert GP]]
[[Category: Lee MS]]
[[Category: Soman KV]]
[[Category: Wright PE]]