2iul: Difference between revisions

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[[Image:2iul.jpg|left|200px]]<br /><applet load="2iul" size="350" color="white" frame="true" align="right" spinBox="true"
[[Image:2iul.jpg|left|200px]]
caption="2iul, resolution 2.01&Aring;" />
 
'''HUMAN TACE G13 MUTANT'''<br />
{{Structure
|PDB= 2iul |SIZE=350|CAPTION= <scene name='initialview01'>2iul</scene>, resolution 2.01&Aring;
|SITE= <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene>
|LIGAND= <scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>, <scene name='pdbligand=ACT:ACETATE+ION'>ACT</scene>, <scene name='pdbligand=CL:CHLORIDE+ION'>CL</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
|ACTIVITY=
|GENE=
}}
 
'''HUMAN TACE G13 MUTANT'''
 


==Overview==
==Overview==
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==About this Structure==
==About this Structure==
2IUL 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=NAG:'>NAG</scene>, <scene name='pdbligand=ACT:'>ACT</scene>, <scene name='pdbligand=CL:'>CL</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Site: <scene name='pdbsite=AC1:Zn+Binding+Site+For+Chain+A'>AC1</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUL OCA].  
2IUL is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=2IUL OCA].  


==Reference==
==Reference==
Structure of testis ACE glycosylation mutants and evidence for conserved domain movement., Watermeyer JM, Sewell BT, Schwager SL, Natesh R, Corradi HR, Acharya KR, Sturrock ED, Biochemistry. 2006 Oct 24;45(42):12654-63. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=17042482 17042482]
Structure of testis ACE glycosylation mutants and evidence for conserved domain movement., Watermeyer JM, Sewell BT, Schwager SL, Natesh R, Corradi HR, Acharya KR, Sturrock ED, Biochemistry. 2006 Oct 24;45(42):12654-63. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/17042482 17042482]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
[[Category: Single protein]]
[[Category: Single protein]]
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[[Category: zinc]]
[[Category: zinc]]


''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 17:56:09 2008''
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 17:33:34 2008''

Revision as of 18:33, 20 March 2008

File:2iul.jpg


PDB ID 2iul

Drag the structure with the mouse to rotate
, resolution 2.01Å
Sites:
Ligands: , , and
Coordinates: save as pdb, mmCIF, xml



HUMAN TACE G13 MUTANT


OverviewOverview

Human angiotensin-converting enzyme is an important drug target for which little structural information has been available until recent years. The slow progress in obtaining a crystal structure was due to the problem of surface glycosylation, a difficulty that has thus far been overcome by the use of a glucosidase-1 inhibitor in the tissue culture medium. However, the prohibitive cost of these inhibitors and incomplete glucosidase inhibition makes alternative routes to minimizing the N-glycan heterogeneity desirable. Here, glycosylation in the testis isoform (tACE) has been reduced by Asn-Gln point mutations at N-glycosylation sites, and the crystal structures of mutants having two and four intact sites have been solved to 2.0 A and 2.8 A, respectively. Both mutants show close structural identity with the wild-type. A hinge mechanism is proposed for substrate entry into the active cleft, based on homology to human ACE2 at the levels of sequence and flexibility. This is supported by normal-mode analysis that reveals intrinsic flexibility about the active site of tACE. Subdomain II, containing bound chloride and zinc ions, is found to have greater stability than subdomain I in the structures of three ACE homologues. Crystallizable glycosylation mutants open up new possibilities for cocrystallization studies to aid the design of novel ACE inhibitors.

DiseaseDisease

Known diseases associated with this structure: Alzheimer disease, susceptibility to OMIM:[106180], Angiotensin I-converting enzyme, benign serum increase OMIM:[106180], Diabetic nephropathy, susceptibility to OMIM:[106180], Myocardial infarction, susceptibility to OMIM:[106180], Renal tubular dysgenesis OMIM:[106180], SARS, progression of OMIM:[106180]

About this StructureAbout this Structure

2IUL is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

ReferenceReference

Structure of testis ACE glycosylation mutants and evidence for conserved domain movement., Watermeyer JM, Sewell BT, Schwager SL, Natesh R, Corradi HR, Acharya KR, Sturrock ED, Biochemistry. 2006 Oct 24;45(42):12654-63. PMID:17042482

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