1fh0

From Proteopedia

(Difference between revisions)

Revision as of 11:09, 28 July 2021

CRYSTAL STRUCTURE OF HUMAN CATHEPSIN V COMPLEXED WITH AN IRREVERSIBLE VINYL SULFONE INHIBITOR

Structural highlights

1fh0 is a 2 chain structure with sequence from Human. Full crystallographic information is available from OCA. For a guided tour on the structure components use FirstGlance.
Ligands:	,
Resources:	FirstGlance, OCA, PDBe, RCSB, PDBsum, ProSAT

Function

[CATL2_HUMAN] Cysteine protease. May have an important role in corneal physiology.^[1] ^[2]

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

Cathepsin V is a lysosomal cysteine protease that is expressed in the thymus, testis and corneal epithelium. We have determined the 1.6 A resolution crystal structure of human cathepsin V associated with an irreversible vinyl sulfone inhibitor. The fold of this enzyme is similar to the fold adopted by other members of the papain superfamily of cysteine proteases. This study provides a framework for understanding the structural basis for cathepsin V's activity and will aid in the design of inhibitors of this enzyme. A comparison of cathepsin V's active site with the active sites of related proteases revealed a number of differences, especially in the S2 and S3 subsites, that could be exploited in identifying specific cathepsin V inhibitors or in identifying inhibitors of other cysteine proteases that would be selective against cathepsin V.

Crystal structure of human cathepsin V.,Somoza JR, Zhan H, Bowman KK, Yu L, Mortara KD, Palmer JT, Clark JM, McGrath ME Biochemistry. 2000 Oct 17;39(41):12543-51. PMID:11027133^[3]

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

References

↑ Adachi W, Kawamoto S, Ohno I, Nishida K, Kinoshita S, Matsubara K, Okubo K. Isolation and characterization of human cathepsin V: a major proteinase in corneal epithelium. Invest Ophthalmol Vis Sci. 1998 Sep;39(10):1789-96. PMID:9727401
↑ Bromme D, Li Z, Barnes M, Mehler E. Human cathepsin V functional expression, tissue distribution, electrostatic surface potential, enzymatic characterization, and chromosomal localization. Biochemistry. 1999 Feb 23;38(8):2377-85. PMID:10029531 doi:10.1021/bi982175f
↑ Somoza JR, Zhan H, Bowman KK, Yu L, Mortara KD, Palmer JT, Clark JM, McGrath ME. Crystal structure of human cathepsin V. Biochemistry. 2000 Oct 17;39(41):12543-51. PMID:11027133

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

Proteopedia Page Contributors and Editors (what is this?)

OCA

Retrieved from "http://52.214.119.220/wiki/index.php/1fh0"

@@ Line 3: / Line 3: @@
 <StructureSection load='1fh0' size='340' side='right'caption='[[1fh0]], [[Resolution|resolution]] 1.60&Aring;' scene=''>
 == Structural highlights ==
-<table><tr><td colspan='2'>[[1fh0]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1FH0 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1FH0 FirstGlance]. <br>
+<table><tr><td colspan='2'>[[1fh0]] is a 2 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=1FH0 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1FH0 FirstGlance]. <br>
-</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=0IW:NALPHA-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-N-[(3S)-1-PHENYL-5-(PHENYLSULFONYL)PENTAN-3-YL]-L-PHENYLALANINAMIDE'>0IW</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
+</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=0IW:NALPHA-[(4-METHYLPIPERAZIN-1-YL)CARBONYL]-N-[(3S)-1-PHENYL-5-(PHENYLSULFONYL)PENTAN-3-YL]-L-PHENYLALANINAMIDE'>0IW</scene>, <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene></td></tr>
-<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1fh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fh0 OCA], [http://pdbe.org/1fh0 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1fh0 RCSB], [http://www.ebi.ac.uk/pdbsum/1fh0 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1fh0 ProSAT]</span></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=1fh0 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1fh0 OCA], [https://pdbe.org/1fh0 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1fh0 RCSB], [https://www.ebi.ac.uk/pdbsum/1fh0 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1fh0 ProSAT]</span></td></tr>
 </table>
 == Function ==
-[[http://www.uniprot.org/uniprot/CATL2_HUMAN CATL2_HUMAN]] Cysteine protease. May have an important role in corneal physiology.<ref>PMID:9727401</ref> <ref>PMID:10029531</ref>
+[[https://www.uniprot.org/uniprot/CATL2_HUMAN CATL2_HUMAN]] Cysteine protease. May have an important role in corneal physiology.<ref>PMID:9727401</ref> <ref>PMID:10029531</ref>
 == Evolutionary Conservation ==
 [[Image:Consurf_key_small.gif|200px|right]]

1fh0

From Proteopedia

Revision as of 11:09, 28 July 2021

CRYSTAL STRUCTURE OF HUMAN CATHEPSIN V COMPLEXED WITH AN IRREVERSIBLE VINYL SULFONE INHIBITOR

Structural highlights

Function

Evolutionary Conservation

Publication Abstract from PubMed

See Also

References

Contents

Proteopedia Page Contributors and Editors (what is this?)

Views

Personal tools

Navigation

Search

Toolbox