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[[Image:3ljt.png|left|200px]]
[[Image:3ljt.png|left|200px]]


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{{STRUCTURE_3ljt|  PDB=3ljt  |  SCENE=  }}  
{{STRUCTURE_3ljt|  PDB=3ljt  |  SCENE=  }}  


===Crystal Structure of the Catalytic Domain of ADAMTS-5 in Complex with an Amino-2-indanol compound===
===Crystal Structure of the Catalytic Domain of ADAMTS-5 in Complex with an Amino-2-indanol compound===


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{{ABSTRACT_PUBMED_21370305}}


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==See Also==
==See Also==
*[[A Disintegrin And Metalloproteinase]]
*[[A Disintegrin And Metalloproteinase|A Disintegrin And Metalloproteinase]]
*[[Superoxide Dismutase]]
*[[Superoxide Dismutase|Superoxide Dismutase]]


==Reference==
==Reference==
<ref group="xtra">PMID:21370305</ref><references group="xtra"/>
<ref group="xtra">PMID:021370305</ref><references group="xtra"/>
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Caspers, N.]]
[[Category: Caspers, N.]]
[[Category: Shieh, H S.]]
[[Category: Shieh, H S.]]
[[Category: Williams, J M.]]
[[Category: Williams, J M.]]
[[Category: Alpha/beta structure]]
[[Category: Central five stranded beta-sheet]]
[[Category: Cleavage on pair of basic residue]]
[[Category: Disulfide bond]]
[[Category: Extracellular matrix]]
[[Category: Glycoprotein]]
[[Category: Hydrolase]]
[[Category: Metal-binding]]
[[Category: Metalloprotease]]
[[Category: Protease]]
[[Category: Secreted]]
[[Category: Zymogen]]

Revision as of 22:06, 26 July 2012

File:3ljt.png

Template:STRUCTURE 3ljt

Crystal Structure of the Catalytic Domain of ADAMTS-5 in Complex with an Amino-2-indanol compound

Template:ABSTRACT PUBMED 21370305

About this Structure

3ljt is a 1 chain structure of A Disintegrin And Metalloproteinase and Superoxide Dismutase with sequence from Homo sapiens. Full crystallographic information is available from OCA.

See Also

Reference

  1. Shieh HS, Tomasselli AG, Mathis KJ, Schnute ME, Woodard SS, Caspers N, Williams JM, Kiefer JR, Munie G, Wittwer A, Malfait AM, Tortorella MD. Structure analysis reveals the flexibility of the ADAMTS-5 active site. Protein Sci. 2011 Apr;20(4):735-44. doi: 10.1002/pro.606. PMID:21370305 doi:10.1002/pro.606

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