View source for 1lwa


==Solution Structure of SRY_DNA==
<StructureSection load='1lwa' size='340' side='right'caption='[[1lwa]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[1lwa]] is a 2 chain structure. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LWA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1LWA 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='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=1lwa FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1lwa OCA], [https://pdbe.org/1lwa PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1lwa RCSB], [https://www.ebi.ac.uk/pdbsum/1lwa PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1lwa ProSAT]</span></td></tr>
</table>
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
NHP6A is a non-sequence-specific DNA-binding protein from Saccharomyces cerevisiae which belongs to the HMGB protein family. Previously, we have solved the structure of NHP6A in the absence of DNA and modeled its interaction with DNA. Here, we present the refined solution structures of the NHP6A-DNA complex as well as the free 15bp DNA. Both the free and bound forms of the protein adopt the typical L-shaped HMGB domain fold. The DNA in the complex undergoes significant structural rearrangement from its free form while the protein shows smaller but significant conformational changes in the complex. Structural and mutational analysis as well as comparison of the complex with the free DNA provides insight into the factors that contribute to binding site selection and DNA deformations in the complex. Further insight into the amino acid determinants of DNA binding by HMGB domain proteins is given by a correlation study of NHP6A and 32 other HMGB domains belonging to both the DNA-sequence-specific and non-sequence-specific families of HMGB proteins. The resulting correlations can be rationalized by comparison of solved structures of HMGB proteins.

The S. cerevisiae architectural HMGB protein NHP6A complexed with DNA: DNA and protein conformational changes upon binding.,Masse JE, Wong B, Yen YM, Allain FH, Johnson RC, Feigon J J Mol Biol. 2002 Oct 18;323(2):263-84. PMID:12381320<ref>PMID:12381320</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
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== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Large Structures]]
[[Category: Allain FH-T]]
[[Category: Feigon J]]
[[Category: Johnson RC]]
[[Category: Masse JE]]
[[Category: Wong B]]
[[Category: Yen Y-M]]