1lay
From Proteopedia
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| - | [[Image:1lay.jpg|left|200px]] | + | [[Image:1lay.jpg|left|200px]] |
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| - | '''CRYSTAL STRUCTURE OF CYTOMEGALOVIRUS PROTEASE''' | + | {{Structure |
| + | |PDB= 1lay |SIZE=350|CAPTION= <scene name='initialview01'>1lay</scene>, resolution 2.5Å | ||
| + | |SITE= <scene name='pdbsite=CAT:Catalytic+Triad'>CAT</scene> | ||
| + | |LIGAND= | ||
| + | |ACTIVITY= | ||
| + | |GENE= | ||
| + | }} | ||
| + | |||
| + | '''CRYSTAL STRUCTURE OF CYTOMEGALOVIRUS PROTEASE''' | ||
| + | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
| - | 1LAY is a [ | + | 1LAY is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Cytomegalovirus Cytomegalovirus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1LAY OCA]. |
==Reference== | ==Reference== | ||
| - | Unique fold and active site in cytomegalovirus protease., Qiu X, Culp JS, DiLella AG, Hellmig B, Hoog SS, Janson CA, Smith WW, Abdel-Meguid SS, Nature. 1996 Sep 19;383(6597):275-9. PMID:[http:// | + | Unique fold and active site in cytomegalovirus protease., Qiu X, Culp JS, DiLella AG, Hellmig B, Hoog SS, Janson CA, Smith WW, Abdel-Meguid SS, Nature. 1996 Sep 19;383(6597):275-9. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8805707 8805707] |
[[Category: Cytomegalovirus]] | [[Category: Cytomegalovirus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: viral protease]] | [[Category: viral protease]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 12:28:44 2008'' |
Revision as of 10:28, 20 March 2008
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| , resolution 2.5Å | |||||||
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| Coordinates: | save as pdb, mmCIF, xml | ||||||
CRYSTAL STRUCTURE OF CYTOMEGALOVIRUS PROTEASE
Overview
Human herpesviruses are responsible for a variety of diseases. They are divided into three subfamilies: alpha includes herpes simplex viruses (HSV-1 and HSV-2) and varicella-zoster virus (VZV); beta includes cytomegalovirus (CMV) and human herpesvirus-6 (HHV-6); and gamma includes Epstein-Barr virus (EBV). Each virus encodes a serine protease that is essential for its replication and is a potential target for therapeutic intervention. Human CMV is a ubiquitous opportunistic pathogen that can result in life-threatening infections in congenitally infected infants, immunocompromised individuals and immunosuppressed cancer or transplant patients. Here we report the crystal structure of human CMV protease at 2.5 angstroms resolution. The structure reveals a fold that has not been reported for any other serine protease, and an active site consisting of a novel catalytic triad in which the third member is a histidine instead of an aspartic acid, or possibly a catalytic tetrad consisting of a serine, two histidines and an aspartic acid. An unusual dimer interface that is important to the protease activity has also been identified.
About this Structure
1LAY is a Single protein structure of sequence from Cytomegalovirus. Full crystallographic information is available from OCA.
Reference
Unique fold and active site in cytomegalovirus protease., Qiu X, Culp JS, DiLella AG, Hellmig B, Hoog SS, Janson CA, Smith WW, Abdel-Meguid SS, Nature. 1996 Sep 19;383(6597):275-9. PMID:8805707
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