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1rn7

From Proteopedia

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Current revision

Structure of human cystatin D

Structural highlights

1rn7 is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Method:	X-ray diffraction, Resolution 2.5Å
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

CYTD_HUMAN Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B.^[1]

Evolutionary Conservation

Check, as determined by ConSurfDB. You may read the explanation of the method and the full data available from ConSurf.

Publication Abstract from PubMed

Cystatins are natural inhibitors of papain-like (family C1) and legumain-related (family C13) cysteine peptidases. Cystatin D is a type 2 cystatin, a secreted inhibitor found in human saliva and tear fluid. Compared with its homologues, cystatin D presents an unusual inhibition profile with a preferential inhibition cathepsin S > cathepsin H > cathepsin L and no inhibition of cathepsin B or pig legumain. To elucidate the structural reasons for this specificity, we have crystallized recombinant human Arg(26)-cystatin D and solved its structures at room temperature and at cryo conditions to 2.5- and 1.8-A resolution, respectively. Human cystatin D presents the typical cystatin fold, with a five-stranded anti-parallel beta-sheet wrapped around a five-turn alpha-helix. The structures reveal differences in the peptidase-interacting regions when compared with other cystatins, providing plausible explanations for the restricted inhibitory specificity of cystatin D for some papain-like peptidases and its lack of reactivity toward legumain-related enzymes.

Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile.,Alvarez-Fernandez M, Liang YH, Abrahamson M, Su XD J Biol Chem. 2005 May 6;280(18):18221-8. Epub 2005 Feb 23. PMID:15728581^[2]

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

References

↑ Balbin M, Hall A, Grubb A, Mason RW, Lopez-Otin C, Abrahamson M. Structural and functional characterization of two allelic variants of human cystatin D sharing a characteristic inhibition spectrum against mammalian cysteine proteinases. J Biol Chem. 1994 Sep 16;269(37):23156-62. PMID:8083219
↑ Alvarez-Fernandez M, Liang YH, Abrahamson M, Su XD. Crystal structure of human cystatin D, a cysteine peptidase inhibitor with restricted inhibition profile. J Biol Chem. 2005 May 6;280(18):18221-8. Epub 2005 Feb 23. PMID:15728581 doi:10.1074/jbc.M411914200

1 Structural highlights
2 Function
3 Evolutionary Conservation
4 Publication Abstract from PubMed
5 References

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1rn7"

@@ Line 3: / Line 3: @@
 <StructureSection load='1rn7' size='340' side='right'caption='[[1rn7]], [[Resolution|resolution]] 2.50&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1rn7]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RN7 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1rn7]] 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=1RN7 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1RN7 FirstGlance]. <br>
-</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1roa|1roa]]</div></td></tr>
+</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution|Resolution]] 2.5&#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=1rn7 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1rn7 OCA], [https://pdbe.org/1rn7 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1rn7 RCSB], [https://www.ebi.ac.uk/pdbsum/1rn7 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1rn7 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[https://www.uniprot.org/uniprot/CYTD_HUMAN CYTD_HUMAN]] Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B.<ref>PMID:8083219</ref>
+[https://www.uniprot.org/uniprot/CYTD_HUMAN CYTD_HUMAN] Cysteine proteinase inhibitor that possibly plays a protective role against proteinases present in the oral cavity. The order of preference for inhibition is cathepsin S > cathepsin H > cathepsin L > cathepsin B.<ref>PMID:8083219</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]
@@ Line 32: / Line 32: @@
 __TOC__
 </StructureSection>
-[[Category: Human]]
+[[Category: Homo sapiens]]
 [[Category: Large Structures]]
-[[Category: Abrahamson, M]]
+[[Category: Abrahamson M]]
-[[Category: Alvarez-Fernandez, M]]
+[[Category: Alvarez-Fernandez M]]
-[[Category: Liang, Y H]]
+[[Category: Liang YH]]
-[[Category: Su, X D]]
+[[Category: Su XD]]
-[[Category: Cystatin d]]
-[[Category: Inhibitor of cysteine peptidase]]
-[[Category: Protein binding]]

1rn7

From Proteopedia

Current revision

Structure of human cystatin D

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

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