1r64

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[[Image:1r64.jpg|left|200px]]<br /><applet load="1r64" size="350" color="white" frame="true" align="right" spinBox="true"
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[[Image:1r64.jpg|left|200px]]
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caption="1r64, resolution 2.20&Aring;" />
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'''The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor'''<br />
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{{Structure
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|PDB= 1r64 |SIZE=350|CAPTION= <scene name='initialview01'>1r64</scene>, resolution 2.20&Aring;
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|SITE=
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|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=K:POTASSIUM+ION'>K</scene>, <scene name='pdbligand=ACE:ACETYL+GROUP'>ACE</scene> and <scene name='pdbligand=BTB:2-[BIS-(2-HYDROXY-ETHYL)-AMINO]-2-HYDROXYMETHYL-PROPANE-1,3-DIOL'>BTB</scene>
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|ACTIVITY= [http://en.wikipedia.org/wiki/Kexin Kexin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.61 3.4.21.61]
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|GENE= KEX2 OR QDS1 OR YNL238W OR N1122 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=4932 Saccharomyces cerevisiae])
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}}
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'''The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor'''
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==Overview==
==Overview==
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==About this Structure==
==About this Structure==
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1R64 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae] with <scene name='pdbligand=NAG:'>NAG</scene>, <scene name='pdbligand=CA:'>CA</scene>, <scene name='pdbligand=K:'>K</scene>, <scene name='pdbligand=ACE:'>ACE</scene> and <scene name='pdbligand=BTB:'>BTB</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Kexin Kexin], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=3.4.21.61 3.4.21.61] Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R64 OCA].
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1R64 is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Saccharomyces_cerevisiae Saccharomyces cerevisiae]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R64 OCA].
==Reference==
==Reference==
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Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases., Holyoak T, Kettner CA, Petsko GA, Fuller RS, Ringe D, Biochemistry. 2004 Mar 9;43(9):2412-21. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=14992578 14992578]
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Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases., Holyoak T, Kettner CA, Petsko GA, Fuller RS, Ringe D, Biochemistry. 2004 Mar 9;43(9):2412-21. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/14992578 14992578]
[[Category: Kexin]]
[[Category: Kexin]]
[[Category: Saccharomyces cerevisiae]]
[[Category: Saccharomyces cerevisiae]]
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[[Category: subtilisin]]
[[Category: subtilisin]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:47:28 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 13:47:20 2008''

Revision as of 11:47, 20 March 2008

Image:1r64.jpg


PDB ID 1r64

Drag the structure with the mouse to rotate
, resolution 2.20Å
Ligands: , , , and
Gene: KEX2 OR QDS1 OR YNL238W OR N1122 (Saccharomyces cerevisiae)
Activity: Kexin, with EC number 3.4.21.61
Coordinates: save as pdb, mmCIF, xml



The 2.2 A crystal structure of Kex2 protease in complex with Ac-Arg-Glu-Lys-boroArg peptidyl boronic acid inhibitor


Overview

Kex2 is the yeast prototype of a large family of serine proteases that are highly specific for cleavage of their peptide substrates C-terminal to paired basic sites. This paper reports the 2.2 A resolution crystal structure of ssKex2 in complex with an Ac-Arg-Glu-Lys-Arg peptidyl boronic acid inhibitor (R = 19.7, R(free) = 23.4). By comparison of this structure with the structure of the mammalian homologue furin [Henrich, S., et al. (2003) Nat. Struct. Biol. 10, 520-526], we suggest a structural basis for the differences in substrate recognition at the P(2) and P(4) positions between Kex2 and furin and provide a structural rationale for the lack of P(6) recognition in Kex2. In addition, several monovalent cation binding sites are identified, and a mechanism of activation of Kex2 by potassium ion is proposed.

About this Structure

1R64 is a Single protein structure of sequence from Saccharomyces cerevisiae. Full crystallographic information is available from OCA.

Reference

Structural basis for differences in substrate selectivity in Kex2 and furin protein convertases., Holyoak T, Kettner CA, Petsko GA, Fuller RS, Ringe D, Biochemistry. 2004 Mar 9;43(9):2412-21. PMID:14992578

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