This old version of Proteopedia is provided for student assignments while the new version is undergoing repairs. Content and edits done in this old version of Proteopedia after March 1, 2026 will eventually be lost when it is retired in about June of 2026.


Apply for new accounts at the new Proteopedia. Your logins will work in both the old and new versions.


5znf

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
(New page: 200px<br /> <applet load="5znf" size="450" color="white" frame="true" align="right" spinBox="true" caption="5znf" /> '''ALTERNATING ZINC FINGERS IN THE HUMAN MALE ...)
Current revision (10:06, 22 May 2024) (edit) (undo)
 
(12 intermediate revisions not shown.)
Line 1: Line 1:
-
[[Image:5znf.gif|left|200px]]<br />
 
-
<applet load="5znf" size="450" color="white" frame="true" align="right" spinBox="true"
 
-
caption="5znf" />
 
-
'''ALTERNATING ZINC FINGERS IN THE HUMAN MALE ASSOCIATED PROTEIN ZFY: 2D NMR STRUCTURE OF AN EVEN FINGER AND IMPLICATIONS FOR "JUMPING-LINKER" DNA RECOGNITION'''<br />
 
-
==Overview==
+
==ALTERNATING ZINC FINGERS IN THE HUMAN MALE ASSOCIATED PROTEIN ZFY: 2D NMR STRUCTURE OF AN EVEN FINGER AND IMPLICATIONS FOR "JUMPING-LINKER" DNA RECOGNITION==
-
ZFY, a sex-related Zn-finger protein encoded by the human Y chromosome, is, distinguished from the general class of Zn-finger proteins by the presence, of a two-finger repeat. Whereas odd-numbered domains and linkers fit a, general consensus, even-numbered domains and linkers exhibit systematic, differences. Because this alternation may have fundamental implications, for the mechanism of protein-DNA recognition, we have undertaken, biochemical and structural studies of fragments of ZFY. We describe here, the solution structure of a representative nonconsensus (even-numbered) Zn, finger based on 2D NMR studies of a 30-residue peptide. Structural, modeling by distance geometry and simulated annealing (DG/SA) demonstrates, that this peptide folds as a miniglobular domain containing a C-terminal, beta--hairpin and N-terminal alpha-helix (beta beta alpha motif). These, features are similar to (but not identical with) those previously, described in consensus-type Zn fingers (derived from ADR1 and Xfin); the, similarities suggest that even and odd ZFY domains bind DNA by a common, mechanism. A model of the protein-DNA complex (designated the, "jumping-linker" model) is presented and discussed in terms of the ZFY, two-finger repeat. In this model every other linker is proposed to cross, the minor groove by means of a putative finger/linker submotif, HX4HX3-hydrophobic residue-X3. Analogous use of a hydrophobic residue in a, linker that spans the minor groove has recently been described in, crystallographic and 3D NMR studies of homeodomain-DNA complexes. The, proposed model of ZFY is supported in part by the hydroxyl radical, footprint of the TFIIIA-DNA complex [Churchill, M.E.A., Tullius, T.D., &amp;, Klug, A. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 5528-5532].
+
<StructureSection load='5znf' size='340' side='right'caption='[[5znf]]' scene=''>
 +
== Structural highlights ==
 +
<table><tr><td colspan='2'>[[5znf]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5ZNF OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5ZNF 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=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=5znf FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5znf OCA], [https://pdbe.org/5znf PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5znf RCSB], [https://www.ebi.ac.uk/pdbsum/5znf PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5znf ProSAT]</span></td></tr>
 +
</table>
 +
== Function ==
 +
[https://www.uniprot.org/uniprot/ZFY_HUMAN ZFY_HUMAN] Probable transcriptional activator. Binds to the consensus sequence 5'-AGGCCY-3'.
 +
== Evolutionary Conservation ==
 +
[[Image:Consurf_key_small.gif|200px|right]]
 +
Check<jmol>
 +
<jmolCheckbox>
 +
<scriptWhenChecked>; select protein; define ~consurf_to_do selected; consurf_initial_scene = true; script "/wiki/ConSurf/zn/5znf_consurf.spt"</scriptWhenChecked>
 +
<scriptWhenUnchecked>script /wiki/extensions/Proteopedia/spt/initialview01.spt</scriptWhenUnchecked>
 +
<text>to colour the structure by Evolutionary Conservation</text>
 +
</jmolCheckbox>
 +
</jmol>, as determined by [http://consurfdb.tau.ac.il/ ConSurfDB]. You may read the [[Conservation%2C_Evolutionary|explanation]] of the method and the full data available from [http://bental.tau.ac.il/new_ConSurfDB/main_output.php?pdb_ID=5znf ConSurf].
 +
<div style="clear:both"></div>
 +
<div style="background-color:#fffaf0;">
 +
== Publication Abstract from PubMed ==
 +
ZFY, a sex-related Zn-finger protein encoded by the human Y chromosome, is distinguished from the general class of Zn-finger proteins by the presence of a two-finger repeat. Whereas odd-numbered domains and linkers fit a general consensus, even-numbered domains and linkers exhibit systematic differences. Because this alternation may have fundamental implications for the mechanism of protein-DNA recognition, we have undertaken biochemical and structural studies of fragments of ZFY. We describe here the solution structure of a representative nonconsensus (even-numbered) Zn finger based on 2D NMR studies of a 30-residue peptide. Structural modeling by distance geometry and simulated annealing (DG/SA) demonstrates that this peptide folds as a miniglobular domain containing a C-terminal beta--hairpin and N-terminal alpha-helix (beta beta alpha motif). These features are similar to (but not identical with) those previously described in consensus-type Zn fingers (derived from ADR1 and Xfin); the similarities suggest that even and odd ZFY domains bind DNA by a common mechanism. A model of the protein-DNA complex (designated the "jumping-linker" model) is presented and discussed in terms of the ZFY two-finger repeat. In this model every other linker is proposed to cross the minor groove by means of a putative finger/linker submotif HX4HX3-hydrophobic residue-X3. Analogous use of a hydrophobic residue in a linker that spans the minor groove has recently been described in crystallographic and 3D NMR studies of homeodomain-DNA complexes. The proposed model of ZFY is supported in part by the hydroxyl radical footprint of the TFIIIA-DNA complex [Churchill, M.E.A., Tullius, T.D., &amp; Klug, A. (1990) Proc. Natl. Acad. Sci. U.S.A. 87, 5528-5532].
-
==Disease==
+
Alternating zinc fingers in the human male associated protein ZFY: 2D NMR structure of an even finger and implications for "jumping-linker" DNA recognition.,Kochoyan M, Havel TF, Nguyen DT, Dahl CE, Keutmann HT, Weiss MA Biochemistry. 1991 Apr 9;30(14):3371-86. PMID:1849423<ref>PMID:1849423</ref>
-
Known disease associated with this structure: Spastic paraplegia 33 OMIM:[[http://www.ncbi.nlm.nih.gov/entrez/dispomim.cgi?id=610243 610243]]
+
-
==About this Structure==
+
From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
-
5ZNF is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with ZN as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=5ZNF OCA].
+
</div>
-
 
+
<div class="pdbe-citations 5znf" style="background-color:#fffaf0;"></div>
-
==Reference==
+
== References ==
-
Alternating zinc fingers in the human male associated protein ZFY: 2D NMR structure of an even finger and implications for "jumping-linker" DNA recognition., Kochoyan M, Havel TF, Nguyen DT, Dahl CE, Keutmann HT, Weiss MA, Biochemistry. 1991 Apr 9;30(14):3371-86. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=1849423 1849423]
+
<references/>
 +
__TOC__
 +
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
-
[[Category: Single protein]]
+
[[Category: Large Structures]]
-
[[Category: Keutmann, H.T.]]
+
[[Category: Keutmann HT]]
-
[[Category: Kochoyan, M.]]
+
[[Category: Kochoyan M]]
-
[[Category: Weiss, M.A.]]
+
[[Category: Weiss MA]]
-
[[Category: ZN]]
+
-
[[Category: zinc finger dna binding domain]]
+
-
 
+
-
''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 23:52:27 2007''
+

Current revision

ALTERNATING ZINC FINGERS IN THE HUMAN MALE ASSOCIATED PROTEIN ZFY: 2D NMR STRUCTURE OF AN EVEN FINGER AND IMPLICATIONS FOR "JUMPING-LINKER" DNA RECOGNITION

PDB ID 5znf

Drag the structure with the mouse to rotate

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools