View source for 5gva


==WD40 domain of human AND-1==
<StructureSection load='5gva' size='340' side='right'caption='[[5gva]], [[Resolution|resolution]] 1.85&Aring;' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[5gva]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=5GVA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=5GVA FirstGlance]. <br>
</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 1.851&#8491;</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=5gva FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=5gva OCA], [https://pdbe.org/5gva PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=5gva RCSB], [https://www.ebi.ac.uk/pdbsum/5gva PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=5gva ProSAT]</span></td></tr>
</table>
== Function ==
[https://www.uniprot.org/uniprot/WDHD1_HUMAN WDHD1_HUMAN] Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication.<ref>PMID:19805216</ref> 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
DNA replication in eukaryotic cells is performed by a multiprotein complex called the replisome, which consists of helicases, polymerases, and adaptor molecules. Human acidic nucleoplasmic DNA-binding protein 1 (AND-1), also known as WD repeat and high mobility group (HMG)-box DNA-binding protein 1 (WDHD1), is an adaptor molecule crucial for DNA replication. Although structural information for the AND-1 yeast ortholog is available, the mechanistic details for how human AND-1 protein anchors the lagging-strand DNA polymerase alpha (pol alpha) to the DNA helicase complex (Cdc45-MCM2-7-GINS, CMG) await elucidation. Here, we report the structures of the N-terminal WD40 and SepB domains of human AND-1, as well as a biochemical analysis of the C-terminal HMG domain. We show that AND-1 exists as a homotrimer mediated by the SepB domain. Mutant study results suggested that a positively charged groove within the SepB domain provides binding sites for pol alpha. Different from its ortholog protein in budding yeast, human AND-1 is recruited to the CMG complex, mediated by unknown participants other than Go Ichi Ni San. In addition, we show that AND-1 binds to DNA in vitro, using its C-terminal HMG domain. In conclusion, our findings provide important insights into the mechanistic details of human AND-1 function, advancing our understanding of replisome formation during eukaryotic replication.

The structure and polymerase-recognition mechanism of the crucial adaptor protein AND-1 in the human replisome.,Guan C, Li J, Sun D, Liu Y, Liang H J Biol Chem. 2017 Jun 9;292(23):9627-9636. doi: 10.1074/jbc.M116.758524. Epub, 2017 Apr 5. PMID:28381552<ref>PMID:28381552</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 5gva" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Homo sapiens]]
[[Category: Large Structures]]
[[Category: Guan CC]]
[[Category: Li J]]