4hba - Revision history

OCA at 08:08, 3 November 2022

2022-11-03T08:08:33Z

←Older revision		Revision as of 08:08, 3 November 2022
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	==Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond==		==Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond==
-	<StructureSection load='4hba' size='340' side='right' caption='[[4hba]], [[Resolution\|resolution]] 1.76Å' scene=''>	+	<StructureSection load='4hba' size='340' side='right'caption='[[4hba]], [[Resolution\|resolution]] 1.76Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4hba]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HBA OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4HBA FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4hba]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HBA OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4HBA FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene~~></td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
-	~~<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>~~	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[https://proteopedia.org/fgij/fg.htm?mol=4hba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hba OCA], [https://pdbe.org/4hba PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4hba RCSB], [https://www.ebi.ac.uk/pdbsum/4hba PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4hba ProSAT]</span></td></tr>
-	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>	+
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4hba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hba OCA], [~~http~~://pdbe.org/4hba PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4hba RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4hba PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4hba ProSAT]</span></td></tr>	+
	</table>		</table>
	== Disease ==		== Disease ==
-	[~~[http~~://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:[~~http~~://omim.org/entry/259730 259730]]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.<ref>PMID:1928091</ref> <ref>PMID:1542674</ref> <ref>PMID:8834238</ref> <ref>PMID:9143915</ref> <ref>PMID:15300855</ref>	+	[https://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN] Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:[https://omim.org/entry/259730 259730]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.<ref>PMID:1928091</ref> <ref>PMID:1542674</ref> <ref>PMID:8834238</ref> <ref>PMID:9143915</ref> <ref>PMID:15300855</ref>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>	+	[https://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	</div>		</div>
	<div class="pdbe-citations 4hba" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4hba" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Carbonic anhydrase 3D structures\|Carbonic anhydrase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Carbonate dehydratase~~]]	+	[[Category: Homo sapiens]]
-	[[Category: ~~Human~~]]	+	[[Category: Large Structures]]
-	[[Category: Boone~~, C D~~]]	+	[[Category: Boone CD]]
-	[[Category: Habibzadegan, A]]	+	[[Category: Habibzadegan A]]
-	[[Category: McKenna, R]]	+	[[Category: McKenna R]]
-	~~[[Category: Human carbonic anhydrase ii]]~~	+
-	~~[[Category: Lyase]]~~	+
-	~~[[Category: Thermal stability~~]]	+

OCA at 08:38, 15 November 2017

2017-11-15T08:38:09Z

←Older revision		Revision as of 08:38, 15 November 2017
Line 22:		Line 22:
	</div>		</div>
	<div class="pdbe-citations 4hba" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4hba" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Carbonic anhydrase\|Carbonic anhydrase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 20:13, 11 August 2016

2016-08-11T20:13:57Z

←Older revision		Revision as of 20:13, 11 August 2016
Line 1:		Line 1:
		+
	==Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond==		==Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond==
	<StructureSection load='4hba' size='340' side='right' caption='[[4hba]], [[Resolution\|resolution]] 1.76Å' scene=''>		<StructureSection load='4hba' size='340' side='right' caption='[[4hba]], [[Resolution\|resolution]] 1.76Å' scene=''>
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	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>		<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>		<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
-	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hba OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hba RCSB], [http://www.ebi.ac.uk/pdbsum/4hba PDBsum]</span></td></tr>	+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hba OCA], [http://pdbe.org/4hba PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4hba RCSB], [http://www.ebi.ac.uk/pdbsum/4hba PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4hba ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 20:		Line 21:
	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	</div>		</div>
		+	<div class="pdbe-citations 4hba" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==

OCA at 13:12, 4 January 2015

2015-01-04T13:12:21Z

←Older revision		Revision as of 13:12, 4 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_4hba\| PDB=4hba \| SCENE= }}~~	+	==Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond==
-	===Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond===	+	<StructureSection load='4hba' size='340' side='right' caption='[[4hba]], [[Resolution\|resolution]] 1.76Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23897465}}~~	+	== Structural highlights ==
-		+	<table><tr><td colspan='2'>[[4hba]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HBA OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4HBA FirstGlance]. <br>
-	==Disease==	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=GOL:GLYCEROL'>GOL</scene>, <scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CA2 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
		+	<tr id='activity'><td class="sblockLbl"><b>Activity:</b></td><td class="sblockDat"><span class='plainlinks'>[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] </span></td></tr>
		+	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4hba FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4hba OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4hba RCSB], [http://www.ebi.ac.uk/pdbsum/4hba PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
	[[http://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:[http://omim.org/entry/259730 259730]]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.<ref>PMID:1928091</ref> <ref>PMID:1542674</ref> <ref>PMID:8834238</ref> <ref>PMID:9143915</ref> <ref>PMID:15300855</ref>		[[http://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:[http://omim.org/entry/259730 259730]]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.<ref>PMID:1928091</ref> <ref>PMID:1542674</ref> <ref>PMID:8834238</ref> <ref>PMID:9143915</ref> <ref>PMID:15300855</ref>
-		+	== Function ==
-	==Function==	+
	[[http://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>		[[http://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The carbonic anhydrases (CAs) are a family of mostly zinc metalloenzymes that catalyze the reversible hydration of CO2 to bicarbonate and a proton. Recently, there has been industrial interest in utilizing CAs as biocatalysts for carbon sequestration and biofuel production. The conditions used in these processes, however, result in high temperatures and acidic pH. This unfavorable environment results in rapid destabilization and loss of catalytic activity in CAs, ultimately resulting in cost-inefficient high-maintenance operation of the system. In order to negate these detrimental industrial conditions, cysteines at residues 23 (Ala23Cys) and 203 (Leu203Cys) were engineered into a wild-type variant of human CA II (HCAII) containing the mutation Cys206Ser. The X-ray crystallographic structure of the disulfide-containing HCAII (dsHCAII) was solved to 1.77 A resolution and revealed that successful oxidation of the cysteine bond was achieved while also retaining desirable active-site geometry. Kinetic studies utilizing the measurement of (18)O-labeled CO2 by mass spectrometry revealed that dsHCAII retained high catalytic efficiency, and differential scanning calorimetry showed acid stability and thermal stability that was enhanced by up to 14 K compared with native HCAII. Together, these studies have shown that dsHCAII has properties that could be used in an industrial setting to help to lower costs and improve the overall reaction efficiency.

-	~~==About this Structure==~~	+	Structural and catalytic characterization of a thermally stable and acid-stable variant of human carbonic anhydrase II containing an engineered disulfide bond.,Boone CD, Habibzadegan A, Tu C, Silverman DN, McKenna R Acta Crystallogr D Biol Crystallogr. 2013 Aug;69(Pt 8):1414-22. doi:, 10.1107/S0907444913008743. Epub 2013 Jul 13. PMID:23897465<ref>PMID:23897465</ref>
-	~~[[4hba]] is~~ a ~~1 chain structure with sequence from [http~~:~~//en~~.~~wikipedia~~.~~org~~/~~wiki/Human Human]~~. ~~Full crystallographic information is available from [http~~://~~oca~~.~~weizmann~~.ac.il/~~oca-bin/ocashort?id=4HBA OCA].~~	+
		+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
		+	</div>

	==See Also==		==See Also==
	*[[Carbonic anhydrase\|Carbonic anhydrase]]		*[[Carbonic anhydrase\|Carbonic anhydrase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	~~<ref group="xtra">PMID:023897465</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
	[[Category: Human]]		[[Category: Human]]
-	[[Category: Boone, C D.]]	+	[[Category: Boone, C D]]
-	[[Category: Habibzadegan, A.]]	+	[[Category: Habibzadegan, A]]
-	[[Category: McKenna, R.]]	+	[[Category: McKenna, R]]
	[[Category: Human carbonic anhydrase ii]]		[[Category: Human carbonic anhydrase ii]]
	[[Category: Lyase]]		[[Category: Lyase]]
	[[Category: Thermal stability]]		[[Category: Thermal stability]]

OCA at 07:00, 15 January 2014

2014-01-15T07:00:35Z

←Older revision		Revision as of 07:00, 15 January 2014
Line 1:		Line 1:
	{{STRUCTURE_4hba\| PDB=4hba \| SCENE= }}		{{STRUCTURE_4hba\| PDB=4hba \| SCENE= }}
	===Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond===		===Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond===
		+	{{ABSTRACT_PUBMED_23897465}}

	==Disease==		==Disease==
Line 9:		Line 10:

	==About this Structure==		==About this Structure==
-	[[4hba]] is a 1 chain structure with 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=4HBA OCA].	+	[[4hba]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4HBA OCA].
		+
		+	==See Also==
		+	*[[Carbonic anhydrase\|Carbonic anhydrase]]

	==Reference==		==Reference==
-	<references group="xtra"/><references/>	+	<ref group="xtra">PMID:023897465</ref><references group="xtra"/><references/>
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Boone, C D.]]		[[Category: Boone, C D.]]
	[[Category: Habibzadegan, A.]]		[[Category: Habibzadegan, A.]]

OCA at 05:17, 1 August 2013

2013-08-01T05:17:30Z

←Older revision		Revision as of 05:17, 1 August 2013
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	{{STRUCTURE_4hba\| PDB=4hba \| SCENE= }}
		+	===Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond===

-	~~The~~ entry ~~4hba~~ is ~~ON HOLD~~ ~~until Paper Publication~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Defects in CA2 are the cause of osteopetrosis autosomal recessive type 3 (OPTB3) [MIM:[http://omim.org/entry/259730 259730]]; also known as osteopetrosis with renal tubular acidosis, carbonic anhydrase II deficiency syndrome, Guibaud-Vainsel syndrome or marble brain disease. Osteopetrosis is a rare genetic disease characterized by abnormally dense bone, due to defective resorption of immature bone. The disorder occurs in two forms: a severe autosomal recessive form occurring in utero, infancy, or childhood, and a benign autosomal dominant form occurring in adolescence or adulthood. Autosomal recessive osteopetrosis is usually associated with normal or elevated amount of non-functional osteoclasts. OPTB3 is associated with renal tubular acidosis, cerebral calcification (marble brain disease) and in some cases with mental retardation.<ref>PMID:1928091</ref> <ref>PMID:1542674</ref> <ref>PMID:8834238</ref> <ref>PMID:9143915</ref> <ref>PMID:15300855</ref>

-	~~Authors~~: ~~Boone, C~~.D.~~, Habibzadegan, A~~.~~, McKenna, R~~.	+	==Function==
		+	[[http://www.uniprot.org/uniprot/CAH2_HUMAN CAH2_HUMAN]] Essential for bone resorption and osteoclast differentiation (By similarity). Reversible hydration of carbon dioxide. Can hydrate cyanamide to urea. Involved in the regulation of fluid secretion into the anterior chamber of the eye.<ref>PMID:10550681</ref> <ref>PMID:11831900</ref>

-	~~Description: Structural and Catalytic Characterization of~~ a ~~Thermal and Acid Stable Variant of~~ Human ~~Carbonic Anhydrase II Containing an Engineered Disulfide Bond~~	+	==About this Structure==
		+	[[4hba]] is a 1 chain structure with 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=4HBA OCA].
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Carbonate dehydratase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Boone, C D.]]
		+	[[Category: Habibzadegan, A.]]
		+	[[Category: McKenna, R.]]
		+	[[Category: Human carbonic anhydrase ii]]
		+	[[Category: Lyase]]
		+	[[Category: Thermal stability]]

OCA at 06:58, 10 October 2012

2012-10-10T06:58:20Z

←Older revision		Revision as of 06:58, 10 October 2012
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 4hba is ON HOLD	+	The entry 4hba is ON HOLD until Paper Publication

	Authors: Boone, C.D., Habibzadegan, A., McKenna, R.		Authors: Boone, C.D., Habibzadegan, A., McKenna, R.

	Description: Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond		Description: Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond

OCA: Protected "4hba" [edit=sysop:move=sysop]

2012-10-03T05:52:23Z

Protected "4hba" [edit=sysop:move=sysop]

←Older revision

Revision as of 05:52, 3 October 2012

OCA: New page: '''Unreleased structure''' The entry 4hba is ON HOLD Authors: Boone, C.D., Habibzadegan, A., McKenna, R. Description: Structural and Catalytic Characterization of a Thermal and Acid St...

2012-10-03T05:52:22Z

New page: '''Unreleased structure''' The entry 4hba is ON HOLD Authors: Boone, C.D., Habibzadegan, A., McKenna, R. Description: Structural and Catalytic Characterization of a Thermal and Acid St...

New page

'''Unreleased structure'''

The entry 4hba is ON HOLD

Authors: Boone, C.D., Habibzadegan, A., McKenna, R.

Description: Structural and Catalytic Characterization of a Thermal and Acid Stable Variant of Human Carbonic Anhydrase II Containing an Engineered Disulfide Bond