4au4: Difference between revisions
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==Crystal Structure of Hsp47== | |||
<StructureSection load='4au4' size='340' side='right'caption='[[4au4]], [[Resolution|resolution]] 2.97Å' scene=''> | |||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[4au4]] is a 7 chain structure with sequence from [https://en.wikipedia.org/wiki/Canis_lupus_familiaris Canis lupus familiaris]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4AU4 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4AU4 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]] 2.97Å</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=4au4 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4au4 OCA], [https://pdbe.org/4au4 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4au4 RCSB], [https://www.ebi.ac.uk/pdbsum/4au4 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4au4 ProSAT]</span></td></tr> | |||
</table> | |||
== Function == | |||
[https://www.uniprot.org/uniprot/C7C419_CANLF C7C419_CANLF] Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.[ARBA:ARBA00025405] | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Collagen is the most abundant protein in animals and is a major component of the extracellular matrix in tissues such as skin and bone. A distinctive structural feature of all collagen types is a unique triple-helical structure formed by tandem repeats of the consensus sequence Xaa-Yaa-Gly, in which Xaa and Yaa frequently are proline and hydroxyproline, respectively. Hsp47/SERPINH1 is a procollagen-specific molecular chaperone that, unlike other chaperones, specifically recognizes the folded conformation of its client. Reduced functional levels of Hsp47 were reported in severe recessive forms of osteogenesis imperfecta, and homozygous knockout is lethal in mice. Here we present crystal structures of Hsp47 in its free form and in complex with homotrimeric synthetic collagen model peptides, each comprising one Hsp47-binding site represented by an arginine at the Yaa-position of a Xaa-Yaa-Gly triplet. Two of these three binding sites in the triple helix are occupied by Hsp47 molecules, which bind in a head-to-head fashion, thus making extensive contacts with the leading and trailing strands of the collagen triple helix. The important arginine residue within the Xaa-Arg-Gly triplet is recognized by a conserved aspartic acid. The structures explain the stabilization of the triple helix as well as the inhibition of collagen-bundle formation by Hsp47. In addition, we propose a pH-dependent substrate release mechanism based on a cluster of histidine residues. | |||
Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition.,Widmer C, Gebauer JM, Brunstein E, Rosenbaum S, Zaucke F, Drogemuller C, Leeb T, Baumann U Proc Natl Acad Sci U S A. 2012 Jul 30. PMID:22847422<ref>PMID:22847422</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
<div class="pdbe-citations 4au4" style="background-color:#fffaf0;"></div> | |||
== | ==See Also== | ||
[[ | *[[Heat Shock Protein structures|Heat Shock Protein structures]] | ||
== References == | |||
== | <references/> | ||
< | __TOC__ | ||
</StructureSection> | |||
[[Category: Canis lupus familiaris]] | [[Category: Canis lupus familiaris]] | ||
[[Category: Baumann | [[Category: Large Structures]] | ||
[[Category: Brunstein | [[Category: Baumann U]] | ||
[[Category: Drogemuller | [[Category: Brunstein E]] | ||
[[Category: Gebauer | [[Category: Drogemuller C]] | ||
[[Category: Leeb | [[Category: Gebauer JM]] | ||
[[Category: Rodenbaum | [[Category: Leeb T]] | ||
[[Category: Widmer | [[Category: Rodenbaum S]] | ||
[[Category: Zaucke | [[Category: Widmer C]] | ||
[[Category: Zaucke F]] | |||
Latest revision as of 13:53, 9 May 2024
Crystal Structure of Hsp47Crystal Structure of Hsp47
Structural highlights
FunctionC7C419_CANLF Binds specifically to collagen. Could be involved as a chaperone in the biosynthetic pathway of collagen.[ARBA:ARBA00025405] Publication Abstract from PubMedCollagen is the most abundant protein in animals and is a major component of the extracellular matrix in tissues such as skin and bone. A distinctive structural feature of all collagen types is a unique triple-helical structure formed by tandem repeats of the consensus sequence Xaa-Yaa-Gly, in which Xaa and Yaa frequently are proline and hydroxyproline, respectively. Hsp47/SERPINH1 is a procollagen-specific molecular chaperone that, unlike other chaperones, specifically recognizes the folded conformation of its client. Reduced functional levels of Hsp47 were reported in severe recessive forms of osteogenesis imperfecta, and homozygous knockout is lethal in mice. Here we present crystal structures of Hsp47 in its free form and in complex with homotrimeric synthetic collagen model peptides, each comprising one Hsp47-binding site represented by an arginine at the Yaa-position of a Xaa-Yaa-Gly triplet. Two of these three binding sites in the triple helix are occupied by Hsp47 molecules, which bind in a head-to-head fashion, thus making extensive contacts with the leading and trailing strands of the collagen triple helix. The important arginine residue within the Xaa-Arg-Gly triplet is recognized by a conserved aspartic acid. The structures explain the stabilization of the triple helix as well as the inhibition of collagen-bundle formation by Hsp47. In addition, we propose a pH-dependent substrate release mechanism based on a cluster of histidine residues. Molecular basis for the action of the collagen-specific chaperone Hsp47/SERPINH1 and its structure-specific client recognition.,Widmer C, Gebauer JM, Brunstein E, Rosenbaum S, Zaucke F, Drogemuller C, Leeb T, Baumann U Proc Natl Acad Sci U S A. 2012 Jul 30. PMID:22847422[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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