3o1g: Difference between revisions

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[[Image:3o1g.png|left|200px]]
{{STRUCTURE_3o1g|  PDB=3o1g  |  SCENE=  }}  
{{STRUCTURE_3o1g|  PDB=3o1g  |  SCENE=  }}  
===Cathepsin K covalently bound to a 2-cyano pyrimidine inhibitor with a benzyl P3 group.===
{{ABSTRACT_PUBMED_20843687}}


===Cathepsin K covalently bound to a 2-cyano pyrimidine inhibitor with a benzyl P3 group.===
==Disease==
[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:[http://omim.org/entry/265800 265800]]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.<ref>PMID:8703060</ref><ref>PMID:9529353</ref><ref>PMID:10491211</ref><ref>PMID:10878663</ref>


{{ABSTRACT_PUBMED_20843687}}
==Function==
[[http://www.uniprot.org/uniprot/CATK_HUMAN CATK_HUMAN]] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.


==About this Structure==
==About this Structure==
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==Reference==
==Reference==
<ref group="xtra">PMID:020843687</ref><references group="xtra"/>
<ref group="xtra">PMID:020843687</ref><references group="xtra"/><references/>
[[Category: Cathepsin K]]
[[Category: Cathepsin K]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]

Revision as of 21:20, 24 March 2013

Template:STRUCTURE 3o1g

Cathepsin K covalently bound to a 2-cyano pyrimidine inhibitor with a benzyl P3 group.Cathepsin K covalently bound to a 2-cyano pyrimidine inhibitor with a benzyl P3 group.

Template:ABSTRACT PUBMED 20843687

DiseaseDisease

[CATK_HUMAN] Defects in CTSK are the cause of pycnodysostosis (PKND) [MIM:265800]. PKND is an autosomal recessive osteochondrodysplasia characterized by osteosclerosis and short stature.[1][2][3][4]

FunctionFunction

[CATK_HUMAN] Closely involved in osteoclastic bone resorption and may participate partially in the disorder of bone remodeling. Displays potent endoprotease activity against fibrinogen at acid pH. May play an important role in extracellular matrix degradation.

About this StructureAbout this Structure

3o1g is a 1 chain structure with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See AlsoSee Also

ReferenceReference

[xtra 1]

  1. Rankovic Z, Cai J, Kerr J, Fradera X, Robinson J, Mistry A, Finlay W, McGarry G, Andrews F, Caulfield W, Cumming I, Dempster M, Waller J, Arbuckle W, Anderson M, Martin I, Mitchell A, Long C, Baugh M, Westwood P, Kinghorn E, Jones P, Uitdehaag JC, van Zeeland M, Potin D, Saniere L, Fouquet A, Chevallier F, Deronzier H, Dorleans C, Nicolai E. Optimisation of 2-cyano-pyrimidine inhibitors of cathepsin K: Improving selectivity over hERG. Bioorg Med Chem Lett. 2010 Aug 24. PMID:20843687 doi:10.1016/j.bmcl.2010.08.101
  1. Gelb BD, Shi GP, Chapman HA, Desnick RJ. Pycnodysostosis, a lysosomal disease caused by cathepsin K deficiency. Science. 1996 Aug 30;273(5279):1236-8. PMID:8703060
  2. Gelb BD, Willner JP, Dunn TM, Kardon NB, Verloes A, Poncin J, Desnick RJ. Paternal uniparental disomy for chromosome 1 revealed by molecular analysis of a patient with pycnodysostosis. Am J Hum Genet. 1998 Apr;62(4):848-54. PMID:9529353 doi:S0002-9297(07)60977-X
  3. Ho N, Punturieri A, Wilkin D, Szabo J, Johnson M, Whaley J, Davis J, Clark A, Weiss S, Francomano C. Mutations of CTSK result in pycnodysostosis via a reduction in cathepsin K protein. J Bone Miner Res. 1999 Oct;14(10):1649-53. PMID:10491211
  4. Haagerup A, Hertz JM, Christensen MF, Binderup H, Kruse TA. Cathepsin K gene mutations and 1q21 haplotypes in at patients with pycnodysostosis in an outbred population. Eur J Hum Genet. 2000 Jun;8(6):431-6. PMID:10878663 doi:10.1038/sj.ejhg.5200481

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