3tvn - Revision history

OCA at 10:15, 1 March 2024

OCA — Fri, 01 Mar 2024 10:15:06 GMT

←Older revision		Revision as of 10:15, 1 March 2024
Line 3:		Line 3:
	<StructureSection load='3tvn' size='340' side='right'caption='[[3tvn]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='3tvn' size='340' side='right'caption='[[3tvn]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3tvn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TVN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3tvn]] 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=3TVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TVN FirstGlance]. <br>
-	</td></tr><tr id='~~ligand~~'><td class="sblockLbl"><b>[[~~Ligand~~\|~~Ligands~~:]]</b></td><td class="sblockDat" id="~~ligandDat~~">~~<scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>~~	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">X-ray diffraction, [[Resolution\|Resolution]] 1.497Å</td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max~~-~~height: 3em;'>[[2nxt\|2nxt]]~~, [[~~3tvo~~\|~~3tvo~~]]~~</div>~~</td></tr>	+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><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 ([https://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~~'>~~[https://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [https://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'>[https://proteopedia.org/fgij/fg.htm?mol=3tvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tvn OCA], [https://pdbe.org/3tvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tvn RCSB], [https://www.ebi.ac.uk/pdbsum/3tvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tvn ProSAT]</span></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=3tvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tvn OCA], [https://pdbe.org/3tvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tvn RCSB], [https://www.ebi.ac.uk/pdbsum/3tvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tvn ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[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>	+	[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 ==
-	[[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>	+	[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;">~~	+
-	~~== Publication Abstract from PubMed ==~~	+
-	Variants of human carbonic anhydrase II (HCA II) with amino acid replacements at residues in contact with water molecules in the active-site cavity have provided insights into the proton transfer rates in this protein environment. X-ray crystallography and (18)O exchange measured by membrane inlet mass spectrometry have been used to investigate structural and catalytic properties of variants of HCA II containing replacements of Tyr7 with Phe (Y7F) and Asn67 with Gln (N67Q). The rate constants for transfer of a proton from His64 to the zinc-bound hydroxide during catalysis were 4 and 9 mus(-1) for Y7F and Y7F/N67Q, respectively, compared with a value of 0.8 mus(-1) for wild-type HCA II. These higher values observed for Y7F and Y7F/N67Q HCA II could not be explained by differences in the values of the pK(a) of the proton donor (His64) and acceptor (zinc-bound hydroxide) or by the orientation of the side chain of the proton shuttle residue His64. They appeared to be associated with a reduced level of branching in the networks of hydrogen-bonded water molecules between proton shuttle residue His64 and the zinc-bound solvent molecule as observed in crystal structures at 1.5-1.6 A resolution. Moreover, Y7F/N67Q HCA II is unique among the variants studied in having a direct, hydrogen-bonded chain of water molecules between the zinc-bound solvent and N(epsilon) of His64. This study provides the clearest example to date of the relevance of ordered water structure to rate constants for proton transfer in catalysis by carbonic anhydrase.	+
-		+
-	Water Networks in Fast Proton Transfer during Catalysis by Human Carbonic Anhydrase II.,Mikulski R, West D, Sippel KH, Avvaru BS, Aggarwal M, Tu C, McKenna R, Silverman DN Biochemistry. 2012 Dec 18. PMID:23215152<ref>PMID:23215152</ref>	+
-		+
-	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~	+
-	~~</div>~~	+
-	~~<div class="pdbe-citations 3tvn" style="background-color:#fffaf0;"></div~~>	+

	==See Also==		==See Also==
Line 30:		Line 19:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Carbonate dehydratase]]~~	+	[[Category: Homo sapiens]]
-	~~[[Category: Human~~]]	+
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Avvaru~~, B S~~]]	+	[[Category: Avvaru BS]]
-	[[Category: Chingkuang, T]]	+	[[Category: Chingkuang T]]
-	[[Category: McKenna, R]]	+	[[Category: McKenna R]]
-	[[Category: Mikulski~~, R L~~]]	+	[[Category: Mikulski RL]]
-	[[Category: Sippel~~, K H~~]]	+	[[Category: Sippel KH]]
-	[[Category: West~~, D M]]~~	+	[[Category: West DM]]
-	~~[[Category: Globular protein]]~~	+
-	~~[[Category: Lyase~~]]	+

OCA at 05:47, 13 July 2022

OCA — Wed, 13 Jul 2022 05:47:20 GMT

←Older revision		Revision as of 05:47, 13 July 2022
Line 1:		Line 1:

	==Human Carbonic Anhydrase II Proton Transfer Mutant==		==Human Carbonic Anhydrase II Proton Transfer Mutant==
-	<StructureSection load='3tvn' size='340' side='right' caption='[[3tvn]], [[Resolution\|resolution]] 1.50Å' scene=''>	+	<StructureSection load='3tvn' size='340' side='right'caption='[[3tvn]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3tvn]] 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=3TVN OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=3TVN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3tvn]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3TVN OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=3TVN FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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=ZN:ZINC+ION'>ZN</scene></td></tr>
-	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2nxt\|2nxt]], [[3tvo\|3tvo]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[2nxt\|2nxt]], [[3tvo\|3tvo]]</div></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='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">CA2 ([https://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'>[https://en.wikipedia.org/wiki/Carbonate_dehydratase Carbonate dehydratase], with EC number [https://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=3tvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tvn OCA], [~~http~~://pdbe.org/3tvn PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=3tvn RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/3tvn PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=3tvn ProSAT]</span></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=3tvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tvn OCA], [https://pdbe.org/3tvn PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=3tvn RCSB], [https://www.ebi.ac.uk/pdbsum/3tvn PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=3tvn 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 ==
Line 23:		Line 23:
	</div>		</div>
	<div class="pdbe-citations 3tvn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3tvn" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Carbonic anhydrase 3D structures\|Carbonic anhydrase 3D structures]]
	== References ==		== References ==
	<references/>		<references/>
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	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Avvaru, B S]]		[[Category: Avvaru, B S]]
	[[Category: Chingkuang, T]]		[[Category: Chingkuang, T]]

OCA at 09:56, 8 November 2017

OCA — Wed, 08 Nov 2017 09:56:47 GMT

←Older revision		Revision as of 09:56, 8 November 2017
Line 23:		Line 23:
	</div>		</div>
	<div class="pdbe-citations 3tvn" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 3tvn" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Carbonic anhydrase\|Carbonic anhydrase]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 17:57, 11 August 2016

OCA — Thu, 11 Aug 2016 17:57:56 GMT

←Older revision		Revision as of 17:57, 11 August 2016
Line 1:		Line 1:
		+
	==Human Carbonic Anhydrase II Proton Transfer Mutant==		==Human Carbonic Anhydrase II Proton Transfer Mutant==
	<StructureSection load='3tvn' size='340' side='right' caption='[[3tvn]], [[Resolution\|resolution]] 1.50Å' scene=''>		<StructureSection load='3tvn' size='340' side='right' caption='[[3tvn]], [[Resolution\|resolution]] 1.50Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[3tvn]] 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=3TVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TVN FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[3tvn]] 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=3TVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TVN FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><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"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2nxt\|2nxt]], [[3tvo\|3tvo]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2nxt\|2nxt]], [[3tvo\|3tvo]]</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 ~~Homo sapiens~~])</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=3tvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tvn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tvn RCSB], [http://www.ebi.ac.uk/pdbsum/3tvn 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=3tvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tvn OCA], [http://pdbe.org/3tvn PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=3tvn RCSB], [http://www.ebi.ac.uk/pdbsum/3tvn PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=3tvn ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 21:		Line 22:
	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 3tvn" style="background-color:#fffaf0;"></div>

	==See Also==		==See Also==
Line 29:		Line 31:
	</StructureSection>		</StructureSection>
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Avvaru, B S]]		[[Category: Avvaru, B S]]
	[[Category: Chingkuang, T]]		[[Category: Chingkuang, T]]

OCA at 08:01, 20 January 2015

OCA — Tue, 20 Jan 2015 08:01:38 GMT

←Older revision		Revision as of 08:01, 20 January 2015
Line 1:		Line 1:
-	~~{{STRUCTURE_3tvn~~\| ~~PDB~~=3tvn \| ~~SCENE~~= }}	+	==Human Carbonic Anhydrase II Proton Transfer Mutant==
-	===~~Human Carbonic Anhydrase~~ II ~~Proton Transfer Mutant~~===	+	<StructureSection load='3tvn' size='340' side='right' caption='[[3tvn]], [[Resolution\|resolution]] 1.50Å' scene=''>
-	~~{{ABSTRACT_PUBMED_23215152}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[3tvn]] 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=3TVN OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3TVN FirstGlance]. <br>
		+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=ZN:ZINC+ION'>ZN</scene></td></tr>
		+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[2nxt\|2nxt]], [[3tvo\|3tvo]]</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 Homo sapiens])</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=3tvn FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3tvn OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3tvn RCSB], [http://www.ebi.ac.uk/pdbsum/3tvn 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>
		+	== 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>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Variants of human carbonic anhydrase II (HCA II) with amino acid replacements at residues in contact with water molecules in the active-site cavity have provided insights into the proton transfer rates in this protein environment. X-ray crystallography and (18)O exchange measured by membrane inlet mass spectrometry have been used to investigate structural and catalytic properties of variants of HCA II containing replacements of Tyr7 with Phe (Y7F) and Asn67 with Gln (N67Q). The rate constants for transfer of a proton from His64 to the zinc-bound hydroxide during catalysis were 4 and 9 mus(-1) for Y7F and Y7F/N67Q, respectively, compared with a value of 0.8 mus(-1) for wild-type HCA II. These higher values observed for Y7F and Y7F/N67Q HCA II could not be explained by differences in the values of the pK(a) of the proton donor (His64) and acceptor (zinc-bound hydroxide) or by the orientation of the side chain of the proton shuttle residue His64. They appeared to be associated with a reduced level of branching in the networks of hydrogen-bonded water molecules between proton shuttle residue His64 and the zinc-bound solvent molecule as observed in crystal structures at 1.5-1.6 A resolution. Moreover, Y7F/N67Q HCA II is unique among the variants studied in having a direct, hydrogen-bonded chain of water molecules between the zinc-bound solvent and N(epsilon) of His64. This study provides the clearest example to date of the relevance of ordered water structure to rate constants for proton transfer in catalysis by carbonic anhydrase.

-	~~==Disease==~~	+	Water Networks in Fast Proton Transfer during Catalysis by Human Carbonic Anhydrase II.,Mikulski R, West D, Sippel KH, Avvaru BS, Aggarwal M, Tu C, McKenna R, Silverman DN Biochemistry. 2012 Dec 18. PMID:23215152<ref>PMID:23215152</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==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[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>
-		+
-	~~==About this Structure==~~	+
-	[[3tvn]] 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=3TVN OCA].	+

	==See Also==		==See Also==
	*[[Carbonic anhydrase\|Carbonic anhydrase]]		*[[Carbonic anhydrase\|Carbonic anhydrase]]
-		+	== References ==
-	==~~Reference~~==	+	<references/>
-	<references ~~group="xtra"~~/><~~references~~/>	+	__TOC__
		+	</StructureSection>
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Avvaru, B S.]]	+	[[Category: Avvaru, B S]]
-	[[Category: Chingkuang, T.]]	+	[[Category: Chingkuang, T]]
-	[[Category: McKenna, R.]]	+	[[Category: McKenna, R]]
-	[[Category: Mikulski, R L.]]	+	[[Category: Mikulski, R L]]
-	[[Category: Sippel, K H.]]	+	[[Category: Sippel, K H]]
-	[[Category: West, D M.]]	+	[[Category: West, D M]]
	[[Category: Globular protein]]		[[Category: Globular protein]]
	[[Category: Lyase]]		[[Category: Lyase]]

OCA at 03:31, 25 March 2013

OCA — Mon, 25 Mar 2013 03:31:54 GMT

←Older revision		Revision as of 03:31, 25 March 2013
Line 1:		Line 1:
-	[[Image:3tvn.png\|left\|200px]]
-
	{{STRUCTURE_3tvn\| PDB=3tvn \| SCENE= }}		{{STRUCTURE_3tvn\| PDB=3tvn \| SCENE= }}
-
	===Human Carbonic Anhydrase II Proton Transfer Mutant===		===Human Carbonic Anhydrase II Proton Transfer Mutant===
-
	{{ABSTRACT_PUBMED_23215152}}		{{ABSTRACT_PUBMED_23215152}}
		+
		+	==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>
		+
		+	==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>

	==About this Structure==		==About this Structure==
Line 12:		Line 14:
	==See Also==		==See Also==
	*[[Carbonic anhydrase\|Carbonic anhydrase]]		*[[Carbonic anhydrase\|Carbonic anhydrase]]
		+
		+	==Reference==
		+	<references group="xtra"/><references/>
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 11:37, 30 January 2013

OCA — Wed, 30 Jan 2013 11:37:38 GMT

←Older revision		Revision as of 11:37, 30 January 2013
Line 9:		Line 9:
	==About this Structure==		==About this Structure==
	[[3tvn]] 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=3TVN OCA].		[[3tvn]] 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=3TVN OCA].
		+
		+	==See Also==
		+	*[[Carbonic anhydrase\|Carbonic anhydrase]]
	[[Category: Carbonate dehydratase]]		[[Category: Carbonate dehydratase]]
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]

OCA at 08:10, 2 January 2013

OCA — Wed, 02 Jan 2013 08:10:42 GMT

←Older revision		Revision as of 08:10, 2 January 2013
Line 1:		Line 1:
-	[[Image:3tvn.~~jpg~~\|left\|200px]]	+	[[Image:3tvn.png\|left\|200px]]

	{{STRUCTURE_3tvn\| PDB=3tvn \| SCENE= }}		{{STRUCTURE_3tvn\| PDB=3tvn \| SCENE= }}
Line 5:		Line 5:
	===Human Carbonic Anhydrase II Proton Transfer Mutant===		===Human Carbonic Anhydrase II Proton Transfer Mutant===

		+	{{ABSTRACT_PUBMED_23215152}}

	==About this Structure==		==About this Structure==

OCA at 05:29, 8 August 2012

OCA — Wed, 08 Aug 2012 05:29:02 GMT

←Older revision		Revision as of 05:29, 8 August 2012
Line 1:		Line 1:
-	~~'''Unreleased structure'''~~	+	[[Image:3tvn.jpg\|left\|200px]]

-	~~The entry~~ 3tvn ~~is ON HOLD~~ ~~until Paper Publication~~	+	{{STRUCTURE_3tvn\| PDB=3tvn \| SCENE= }}

-	~~Authors: Mikulski, R.L., West, D.M., Sippel, K.H., Avvaru, B.S., Chingkuang, T., McKenna, R.~~	+	===Human Carbonic Anhydrase II Proton Transfer Mutant===

-	~~Description~~: ~~Human Carbonic Anhydrase II Proton Transfer Mutant~~	+
		+	==About this Structure==
		+	[[3tvn]] 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=3TVN OCA].
		+	[[Category: Carbonate dehydratase]]
		+	[[Category: Homo sapiens]]
		+	[[Category: Avvaru, B S.]]
		+	[[Category: Chingkuang, T.]]
		+	[[Category: McKenna, R.]]
		+	[[Category: Mikulski, R L.]]
		+	[[Category: Sippel, K H.]]
		+	[[Category: West, D M.]]
		+	[[Category: Globular protein]]
		+	[[Category: Lyase]]

OCA at 11:12, 9 November 2011

OCA — Wed, 09 Nov 2011 11:12:53 GMT

←Older revision		Revision as of 11:12, 9 November 2011
Line 1:		Line 1:
	'''Unreleased structure'''		'''Unreleased structure'''

-	The entry 3tvn is ON HOLD	+	The entry 3tvn is ON HOLD until Paper Publication

	Authors: Mikulski, R.L., West, D.M., Sippel, K.H., Avvaru, B.S., Chingkuang, T., McKenna, R.		Authors: Mikulski, R.L., West, D.M., Sippel, K.H., Avvaru, B.S., Chingkuang, T., McKenna, R.

	Description: Human Carbonic Anhydrase II Proton Transfer Mutant		Description: Human Carbonic Anhydrase II Proton Transfer Mutant