1hdj: Difference between revisions
New page: left|200px<br /> <applet load="1hdj" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hdj" /> '''HUMAN HSP40 (HDJ-1), NMR'''<br /> ==Overvi... |
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'''HUMAN HSP40 (HDJ-1), NMR'''<br /> | '''HUMAN HSP40 (HDJ-1), NMR'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
1HDJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http:// | 1HDJ is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HDJ OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: molecular chaperone]] | [[Category: molecular chaperone]] | ||
''Page seeded by [http:// | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri Feb 15 15:56:04 2008'' | ||
Revision as of 16:56, 15 February 2008
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HUMAN HSP40 (HDJ-1), NMR
OverviewOverview
The J-domain is a highly conserved domain found in all members of the DnaJ, family of molecular chaperones. The three-dimensional structure of a, recombinant, uniformly 15N-labeled 77-residue polypeptide containing the, complete J-domain from human Hsp40 (HDJ-1) has been determined by nuclear, magnetic resonance (NMR) spectroscopy in solution. On the basis of 876, upper distance constraints derived from nuclear Overhauser effects (NOE), and 173 dihedral angle constraints, a group of 20 conformers representing, the solution structure of the HDJ-1 J-domain was computed with the program, DIANA and energy-minimized with the program OPAL. The average of the, pairwise root-mean-square deviations of the individual NMR conformers, relative to the mean coordinates for the backbone atoms N, C2 and C' of, residues 4 to 54 and 4 to to 66 is 0.88 and 0.99 A respectively. The, molecular architecture includes four helices composed of residues 5 to 9, 15 to 28, 40 to 54 and 60 to 66. A turn composed of residues 10 to 14, links helices I and II, and a loop composed of residues 29 to 39, containing a highly conserved tripeptide HPD (residues 31 to 33) connects, the antiparallel helices II and III. The tertiary fold formed by helix, I-turn-helix II-loop-helix III forms a closed structural core; the less, defined helix IV stands away from the core of the domain. The side-chains, of the tripeptide HPD extend out from the core of the structure in the, opposite direction from helix IV. The structure supports the hypothesis, that the highly conserved tripeptide could play a key role in the, interaction of Hsp40 with the molecular chaperone, Hsp70.
About this StructureAbout this Structure
1HDJ is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.
ReferenceReference
Nuclear magnetic resonance solution structure of the human Hsp40 (HDJ-1) J-domain., Qian YQ, Patel D, Hartl FU, McColl DJ, J Mol Biol. 1996 Jul 12;260(2):224-35. PMID:8764402
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