1znf: Difference between revisions
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<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1znf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1znf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1znf RCSB], [http://www.ebi.ac.uk/pdbsum/1znf PDBsum]</span></td></tr> | <tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1znf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1znf OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1znf RCSB], [http://www.ebi.ac.uk/pdbsum/1znf PDBsum]</span></td></tr> | ||
</table> | </table> | ||
== Function == | |||
[[http://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;"> | <div style="background-color:#fffaf0;"> | ||
== Publication Abstract from PubMed == | == Publication Abstract from PubMed == | ||
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[[Category: Xenopus laevis]] | [[Category: Xenopus laevis]] | ||
[[Category: Zinc Fingers]] | [[Category: Zinc Fingers]] | ||
[[Category: Case, D A | [[Category: Case, D A]] | ||
[[Category: Gippert, G P | [[Category: Gippert, G P]] | ||
[[Category: Lee, M S | [[Category: Lee, M S]] | ||
[[Category: Soman, K V | [[Category: Soman, K V]] | ||
[[Category: Wright, P E | [[Category: Wright, P E]] | ||
[[Category: Zinc finger dna binding domain]] | [[Category: Zinc finger dna binding domain]] | ||
Revision as of 20:41, 25 December 2014
THREE-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER DNA-BINDING DOMAINTHREE-DIMENSIONAL SOLUTION STRUCTURE OF A SINGLE ZINC FINGER DNA-BINDING DOMAIN
Structural highlights
Function[XFIN_XENLA] Binds to poly-G sequences in RNA. May function in post-translational regulation processes. Publication Abstract from PubMedThe 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[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References |
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