1znc

From Proteopedia

(Difference between revisions)
Jump to: navigation, search
Line 1: Line 1:
-
[[Image:1znc.gif|left|200px]]<br /><applet load="1znc" size="350" color="white" frame="true" align="right" spinBox="true"
+
[[Image:1znc.gif|left|200px]]
-
caption="1znc, resolution 2.8&Aring;" />
+
 
-
'''HUMAN CARBONIC ANHYDRASE IV'''<br />
+
{{Structure
 +
|PDB= 1znc |SIZE=350|CAPTION= <scene name='initialview01'>1znc</scene>, resolution 2.8&Aring;
 +
|SITE= <scene name='pdbsite=CTA:Zn+Coordinated+By+HIS+A+94,+HIS+A+96,+And+HIS+A+119.+Als+...'>CTA</scene> and <scene name='pdbsite=CTB:Zn+Coordinated+By+HIS+B+94,+HIS+B+96,+And+HIS+B+119.+Als+...'>CTB</scene>
 +
|LIGAND= <scene name='pdbligand=SO4:SULFATE+ION'>SO4</scene> and <scene name='pdbligand=ZN:ZINC ION'>ZN</scene>
 +
|ACTIVITY= [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1]
 +
|GENE= HUMAN CAIV ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])
 +
}}
 +
 
 +
'''HUMAN CARBONIC ANHYDRASE IV'''
 +
 
==Overview==
==Overview==
Line 10: Line 19:
==About this Structure==
==About this Structure==
-
1ZNC 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=SO4:'>SO4</scene> and <scene name='pdbligand=ZN:'>ZN</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Active as [http://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [http://www.brenda-enzymes.info/php/result_flat.php4?ecno=4.2.1.1 4.2.1.1] Known structural/functional Sites: <scene name='pdbsite=CTA:Zn+Coordinated+By+HIS+A+94,+HIS+A+96,+And+HIS+A+119.+Als+...'>CTA</scene> and <scene name='pdbsite=CTB:Zn+Coordinated+By+HIS+B+94,+HIS+B+96,+And+HIS+B+119.+Als+...'>CTB</scene>. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ZNC OCA].
+
1ZNC 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=1ZNC OCA].
==Reference==
==Reference==
-
Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution., Stams T, Nair SK, Okuyama T, Waheed A, Sly WS, Christianson DW, Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13589-94. PMID:[http://ispc.weizmann.ac.il//pmbin/getpm?pmid=8942978 8942978]
+
Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution., Stams T, Nair SK, Okuyama T, Waheed A, Sly WS, Christianson DW, Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13589-94. PMID:[http://www.ncbi.nlm.nih.gov/pubmed/8942978 8942978]
[[Category: Carbonate dehydratase]]
[[Category: Carbonate dehydratase]]
[[Category: Homo sapiens]]
[[Category: Homo sapiens]]
Line 27: Line 36:
[[Category: zinc]]
[[Category: zinc]]
-
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 16:17:18 2008''
+
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 15:37:39 2008''

Revision as of 13:37, 20 March 2008


PDB ID 1znc

Drag the structure with the mouse to rotate
, resolution 2.8Å
Sites: and
Ligands: and
Gene: HUMAN CAIV (Homo sapiens)
Activity: Carbonate dehydratase, with EC number 4.2.1.1
Coordinates: save as pdb, mmCIF, xml



HUMAN CARBONIC ANHYDRASE IV


Contents

Overview

It has recently been demonstrated that the C-terminal deletion mutant of recombinant human carbonic anhydrase IV (G267X CA IV) converts the normally glycosylphosphatidylinositol-anchored enzyme into a soluble secretory form which has the same catalytic properties as the membrane-associated enzyme purified from human tissues. We have determined the three-dimensional structure of the secretory form of human CA IV by x-ray crystallographic methods to a resolution of 2.8 A. Although the zinc binding site and the hydrophobic substrate binding pocket of CA IV are generally similar to those of other mammalian isozymes, unique structural differences are found elsewhere in the active site. Two disufide linkages, Cys-6-Cys-11G and Cys-23-Cys-203, stabilize the conformation of the N-terminal domain. The latter disulfide additionally stabilizes an active site loop containing a cis-peptide linkage between Pro-201 and Thr-202 (this loop contains catalytic residue Thr-199). On the opposite side of the active site, the Val-131-Asp-136 segment adopts an extended loop conformation instead of an alpha-helix conformation as found in other isozymes. Finally, the C terminus is surrounded by a substantial electropositive surface potential, which is likely to stabilize the interaction of CA IV with the negatively charged phospholipid headgroups of the membrane. These structural features are unique to CA IV and provide a framework for the design of sulfonamide inhibitors selective for this particular isozyme.

Disease

Known disease associated with this structure: Retinitis pigmentosa-17 OMIM:[114760]

About this Structure

1ZNC is a Single protein structure of sequence from Homo sapiens. Full crystallographic information is available from OCA.

Reference

Crystal structure of the secretory form of membrane-associated human carbonic anhydrase IV at 2.8-A resolution., Stams T, Nair SK, Okuyama T, Waheed A, Sly WS, Christianson DW, Proc Natl Acad Sci U S A. 1996 Nov 26;93(24):13589-94. PMID:8942978

Page seeded by OCA on Thu Mar 20 15:37:39 2008

Proteopedia Page Contributors and Editors (what is this?)

OCA

Personal tools