1m6d

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(New page: 200px<br /> <applet load="1m6d" size="450" color="white" frame="true" align="right" spinBox="true" caption="1m6d, resolution 1.7&Aring;" /> '''Crystal structure of...)
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<applet load="1m6d" size="450" color="white" frame="true" align="right" spinBox="true"
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caption="1m6d, resolution 1.7&Aring;" />
'''Crystal structure of human cathepsin F'''<br />
'''Crystal structure of human cathepsin F'''<br />
==Overview==
==Overview==
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Cathepsin F is a lysosomal cysteine protease of the papain family, and, likely plays a regulatory role in processing the invariant chain that is, associated with the major histocompatibility complex (MHC) class II., Evidence suggests that inhibiting cathepsin F activity will block MHC, class II processing in macrophages. Consequently, inhibitors of this, enzyme may be useful in treating certain diseases that involve an, inappropriate or excessive immune response. We have determined the 1.7A, structure of the mature domain of human cathepsin F associated with an, irreversible vinyl sulfone inhibitor. This structure provides a basis for, understanding cathepsin F's substrate specificity, and suggests ways of, identifying potent and selective inhibitors of this enzyme.
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Cathepsin F is a lysosomal cysteine protease of the papain family, and likely plays a regulatory role in processing the invariant chain that is associated with the major histocompatibility complex (MHC) class II. Evidence suggests that inhibiting cathepsin F activity will block MHC class II processing in macrophages. Consequently, inhibitors of this enzyme may be useful in treating certain diseases that involve an inappropriate or excessive immune response. We have determined the 1.7A structure of the mature domain of human cathepsin F associated with an irreversible vinyl sulfone inhibitor. This structure provides a basis for understanding cathepsin F's substrate specificity, and suggests ways of identifying potent and selective inhibitors of this enzyme.
==About this Structure==
==About this Structure==
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1M6D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with MYP and MYP as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cathepsin_F Cathepsin F], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.41 3.4.22.41] Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1M6D OCA].
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1M6D is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=MYP:'>MYP</scene> and <scene name='pdbligand=MYP:'>MYP</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Cathepsin_F Cathepsin F], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.22.41 3.4.22.41] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1M6D OCA].
==Reference==
==Reference==
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[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: Ho, J.D.]]
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[[Category: Ho, J D.]]
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[[Category: Palmer, J.T.]]
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[[Category: Palmer, J T.]]
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[[Category: Somoza, J.R.]]
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[[Category: Somoza, J R.]]
[[Category: MYP]]
[[Category: MYP]]
[[Category: papain family cysteine protease]]
[[Category: papain family cysteine protease]]
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''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Mon Nov 12 18:08:06 2007''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:51:57 2008''

Revision as of 11:51, 21 February 2008


1m6d, resolution 1.7Å

Drag the structure with the mouse to rotate

Crystal structure of human cathepsin F

Overview

Cathepsin F is a lysosomal cysteine protease of the papain family, and likely plays a regulatory role in processing the invariant chain that is associated with the major histocompatibility complex (MHC) class II. Evidence suggests that inhibiting cathepsin F activity will block MHC class II processing in macrophages. Consequently, inhibitors of this enzyme may be useful in treating certain diseases that involve an inappropriate or excessive immune response. We have determined the 1.7A structure of the mature domain of human cathepsin F associated with an irreversible vinyl sulfone inhibitor. This structure provides a basis for understanding cathepsin F's substrate specificity, and suggests ways of identifying potent and selective inhibitors of this enzyme.

About this Structure

1M6D is a Single protein structure of sequence from Homo sapiens with and as ligands. Active as Cathepsin F, with EC number 3.4.22.41 Full crystallographic information is available from OCA.

Reference

The crystal structure of human cathepsin F and its implications for the development of novel immunomodulators., Somoza JR, Palmer JT, Ho JD, J Mol Biol. 2002 Sep 20;322(3):559-68. PMID:12225749

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