View source for 7dme


==Solution structure of human Aha1==
<StructureSection load='7dme' size='340' side='right'caption='[[7dme]], [[NMR_Ensembles_of_Models | 20 NMR models]]' scene=''>
== Structural highlights ==
<table><tr><td colspan='2'>[[7dme]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=7DME OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=7DME FirstGlance]. <br>
</td></tr><tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">AHSA1, C14orf3, HSPC322 ([https://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</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=7dme FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=7dme OCA], [https://pdbe.org/7dme PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=7dme RCSB], [https://www.ebi.ac.uk/pdbsum/7dme PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=7dme ProSAT]</span></td></tr>
</table>
== Function ==
[[https://www.uniprot.org/uniprot/AHSA1_HUMAN AHSA1_HUMAN]] Cochaperone that stimulates HSP90 ATPase activity (By similarity). May affect a step in the endoplasmic reticulum to Golgi trafficking. 
<div style="background-color:#fffaf0;">
== Publication Abstract from PubMed ==
Aha1 is the only co-chaperone known to strongly stimulate the ATPase activity of Hsp90. Meanwhile, besides the well-studied co-chaperone function, human Aha1 has also been demonstrated to exhibit chaperoning activity against stress-denatured proteins. To provide structural insights for a better understanding of Aha1's co-chaperone and chaperone-like activities, nuclear magnetic resonance (NMR) techniques were used to reveal the unique structure and internal dynamics features of full-length human Aha1. We then found that, in solution, both the two domains of Aha1 presented distinctive thermal stabilities and dynamics behaviors defined by their primary sequences and three-dimensional structures. The low thermal stability (melting temperature of Aha1(28-162): 54.45 degrees C) and the internal dynamics featured with slow motions on the micros-ms time scale were detected for Aha1's N-terminal domain (Aha1N). The aforementioned experimental results suggest that Aha1N is in an energy-unfavorable state, which would therefore thermostatically favor the interaction of Aha1N with its partner proteins such as Hsp90's middle domain. Differently from Aha1N, Aha1C (Aha1's C-terminal domain) exhibited enhanced thermal stability (melting temperature of Aha1(204-335): 72.41 degrees C) and the internal dynamics featured with intermediate motions on the ps-ns time scale. Aha1C's thermal and structural stabilities make it competent for the stabilization of the exposed hydrophobic groove of dimerized Hsp90's N-terminal domain. Of note, according to the NMR data and the thermal shift results, although the very N-terminal region (M1-W27) and the C-terminal relaxin-like factor (RLF) motif showed no tight contacts with the remaining parts of human Aha1, they were identified to play important roles in the recognition of intrinsically disordered pathological alpha-synuclein.

Aha1 Exhibits Distinctive Dynamics Behavior and Chaperone-Like Activity.,Hu H, Wang Q, Du J, Liu Z, Ding Y, Xue H, Zhou C, Feng L, Zhang N Molecules. 2021 Mar 30;26(7). pii: molecules26071943. doi:, 10.3390/molecules26071943. PMID:33808352<ref>PMID:33808352</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>
</div>
<div class="pdbe-citations 7dme" style="background-color:#fffaf0;"></div>
== References ==
<references/>
__TOC__
</StructureSection>
[[Category: Human]]
[[Category: Large Structures]]
[[Category: Hu, H]]
[[Category: Zhang, N]]
[[Category: Zhou, C]]
[[Category: Human activator of hsp90 atpase homolog 1]]
[[Category: Structural protein]]