4oqo - Revision history

OCA at 14:57, 8 November 2023

OCA — Wed, 08 Nov 2023 14:57:48 GMT

←Older revision		Revision as of 14:57, 8 November 2023
Line 4:		Line 4:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4oqo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OQO FirstGlance]. <br>		<table><tr><td colspan='2'>[[4oqo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OQO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</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]] 2.42Å</td></tr>
		+	<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></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=4oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqo OCA], [https://pdbe.org/4oqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oqo RCSB], [https://www.ebi.ac.uk/pdbsum/4oqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oqo 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=4oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqo OCA], [https://pdbe.org/4oqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oqo RCSB], [https://www.ebi.ac.uk/pdbsum/4oqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oqo ProSAT]</span></td></tr>
	</table>		</table>

OCA at 07:40, 25 January 2023

OCA — Wed, 25 Jan 2023 07:40:25 GMT

←Older revision		Revision as of 07:40, 25 January 2023
Line 3:		Line 3:
	<StructureSection load='4oqo' size='340' side='right'caption='[[4oqo]], [[Resolution\|resolution]] 2.42Å' scene=''>		<StructureSection load='4oqo' size='340' side='right'caption='[[4oqo]], [[Resolution\|resolution]] 2.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[4oqo]] is a 2 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4OQO FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[4oqo]] is a 2 chain structure with sequence from [https://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4OQO FirstGlance]. <br>
-	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene>~~</td></tr>~~	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	~~<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3taj\|3taj]]~~</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=4oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqo OCA], [https://pdbe.org/4oqo PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4oqo RCSB], [https://www.ebi.ac.uk/pdbsum/4oqo PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4oqo ProSAT]</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=4oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqo OCA], [~~http~~://pdbe.org/4oqo PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4oqo RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4oqo PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=4oqo ProSAT]</span></td></tr>	+
	</table>		</table>
	== Function ==		== Function ==
-	[~~[http~~://www.uniprot.org/uniprot/TRFL_BOVIN TRFL_BOVIN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref>	+	[https://www.uniprot.org/uniprot/TRFL_BOVIN TRFL_BOVIN] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 28:		Line 27:
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Bhushan, A]]	+	[[Category: Bhushan A]]
-	[[Category: Kaur, P]]	+	[[Category: Kaur P]]
-	[[Category: Pandey, S]]	+	[[Category: Pandey S]]
-	[[Category: Rastogi, N]]	+	[[Category: Rastogi N]]
-	[[Category: Sharma, S]]	+	[[Category: Sharma S]]
-	[[Category: Singh, A]]	+	[[Category: Singh A]]
-	[[Category: Singh~~, T P~~]]	+	[[Category: Singh TP]]
-	[[Category: Sinha, M]]	+	[[Category: Sinha M]]
-	~~[[Category: C-lobe]]~~	+
-	~~[[Category: Hydrolase~~]]	+

OCA at 08:10, 19 February 2020

OCA — Wed, 19 Feb 2020 08:10:25 GMT

←Older revision		Revision as of 08:10, 19 February 2020
Line 1:		Line 1:

	==Crystal structure of the tryptic generated iron-free C-lobe of bovine Lactoferrin at 2.42 Angstrom resolution==		==Crystal structure of the tryptic generated iron-free C-lobe of bovine Lactoferrin at 2.42 Angstrom resolution==
-	<StructureSection load='4oqo' size='340' side='right' caption='[[4oqo]], [[Resolution\|resolution]] 2.42Å' scene=''>	+	<StructureSection load='4oqo' size='340' side='right'caption='[[4oqo]], [[Resolution\|resolution]] 2.42Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4oqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OQO FirstGlance]. <br>		<table><tr><td colspan='2'>[[4oqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OQO FirstGlance]. <br>
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4oqo" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4oqo" style="background-color:#fffaf0;"></div>
		+
		+	==See Also==
		+	*[[Lactoferrin\|Lactoferrin]]
	== References ==		== References ==
	<references/>		<references/>
Line 24:		Line 27:
	</StructureSection>		</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
		+	[[Category: Large Structures]]
	[[Category: Bhushan, A]]		[[Category: Bhushan, A]]
	[[Category: Kaur, P]]		[[Category: Kaur, P]]

OCA at 14:26, 15 November 2017

OCA — Wed, 15 Nov 2017 14:26:00 GMT

←Older revision		Revision as of 14:26, 15 November 2017
Line 19:		Line 19:
	</div>		</div>
	<div class="pdbe-citations 4oqo" style="background-color:#fffaf0;"></div>		<div class="pdbe-citations 4oqo" style="background-color:#fffaf0;"></div>
-
-	==See Also==
-	*[[Lactoferrin\|Lactoferrin]]
	== References ==		== References ==
	<references/>		<references/>

OCA at 16:53, 2 January 2017

OCA — Mon, 02 Jan 2017 16:53:33 GMT

←Older revision		Revision as of 16:53, 2 January 2017
Line 1:		Line 1:
		+
	==Crystal structure of the tryptic generated iron-free C-lobe of bovine Lactoferrin at 2.42 Angstrom resolution==		==Crystal structure of the tryptic generated iron-free C-lobe of bovine Lactoferrin at 2.42 Angstrom resolution==
	<StructureSection load='4oqo' size='340' side='right' caption='[[4oqo]], [[Resolution\|resolution]] 2.42Å' scene=''>		<StructureSection load='4oqo' size='340' side='right' caption='[[4oqo]], [[Resolution\|resolution]] 2.42Å' scene=''>
Line 5:		Line 6:
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3taj\|3taj]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3taj\|3taj]]</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=4oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oqo RCSB], [http://www.ebi.ac.uk/pdbsum/4oqo 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=4oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqo OCA], [http://pdbe.org/4oqo PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4oqo RCSB], [http://www.ebi.ac.uk/pdbsum/4oqo PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=4oqo ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 17:		Line 18:
	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 4oqo" style="background-color:#fffaf0;"></div>

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

OCA at 01:23, 25 December 2014

OCA — Thu, 25 Dec 2014 01:23:13 GMT

←Older revision		Revision as of 01:23, 25 December 2014
Line 3:		Line 3:
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4oqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OQO FirstGlance]. <br>		<table><tr><td colspan='2'>[[4oqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OQO FirstGlance]. <br>
-	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>	+	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene></td></tr>
-	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3taj\|3taj]]</td></tr>	+	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3taj\|3taj]]</td></tr>
-	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oqo RCSB], [http://www.ebi.ac.uk/pdbsum/4oqo 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=4oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oqo RCSB], [http://www.ebi.ac.uk/pdbsum/4oqo PDBsum]</span></td></tr>
-	<table>	+	</table>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/TRFL_BOVIN TRFL_BOVIN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 23:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
-	[[Category: Bhushan, A.]]	+	[[Category: Bhushan, A]]
-	[[Category: Kaur, P.]]	+	[[Category: Kaur, P]]
-	[[Category: Pandey, S.]]	+	[[Category: Pandey, S]]
-	[[Category: Rastogi, N.]]	+	[[Category: Rastogi, N]]
-	[[Category: Sharma, S.]]	+	[[Category: Sharma, S]]
-	[[Category: Singh, A.]]	+	[[Category: Singh, A]]
-	[[Category: Singh, T P.]]	+	[[Category: Singh, T P]]
-	[[Category: Sinha, M.]]	+	[[Category: Sinha, M]]
	[[Category: C-lobe]]		[[Category: C-lobe]]
	[[Category: Hydrolase]]		[[Category: Hydrolase]]

OCA at 09:10, 16 July 2014

OCA — Wed, 16 Jul 2014 09:10:29 GMT

←Older revision		Revision as of 09:10, 16 July 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_4oqo\| PDB=4oqo \| SCENE= }}~~	+	==Crystal structure of the tryptic generated iron-free C-lobe of bovine Lactoferrin at 2.42 Angstrom resolution==
-	===Crystal structure of the tryptic generated iron-free C-lobe of bovine Lactoferrin at 2.42 Angstrom resolution===	+	<StructureSection load='4oqo' size='340' side='right' caption='[[4oqo]], [[Resolution\|resolution]] 2.42Å' scene=''>
		+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[4oqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4OQO FirstGlance]. <br>
		+	</td></tr><tr><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=NAG:N-ACETYL-D-GLUCOSAMINE'>NAG</scene><br>
		+	<tr><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[3taj\|3taj]]</td></tr>
		+	<tr><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4oqo FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4oqo OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4oqo RCSB], [http://www.ebi.ac.uk/pdbsum/4oqo PDBsum]</span></td></tr>
		+	<table>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	Bovine lactoferrin, a 76-kDa glycoprotein (Ala1-Arg689) consists of two similar N- and C-terminal molecular halves with the ability to bind two Fe(3+) ions. The N-terminal half, designated as the N-lobe (Ala1-Arg341) and the C-terminal half designated as the C-lobe (Tyr342-Arg689) have similar iron-binding properties, but the resistant C-lobe prolongs the physiological role of bovine lactoferrin in the digestive tract. Here, we report the crystal structure of true C-lobe, which was produced by limited proteolysis of bovine lactoferrin using trypsin. In the first proteolysis step, two fragments of 21 kDa (Glu86-Lys282) and 45 kDa (Ser283-Arg689) were generated because two lysine residues, Lys85 and Lys282, in the structure of iron-saturated bovine lactoferrin were fully exposed. The 45-kDa fragment was further digested at the newly exposed side chain of Arg341, generating a 38-kDa perfect C-lobe (Tyr342-Arg689). By contrast, the apo-lactoferrin was cut by trypsin only at Arg341, which was exposed in the structure of apo-lactoferrin, whereas the other two sites with Lys85 and Lys282 are inaccessible. The purified iron-saturated C-lobe was crystallized at pH 4.0. The structure was determined by the molecular replacement method using coordinates of the C-terminal half (Arg342-Arg689) of intact camel apo-lactoferrin. The structure determination revealed that the iron atom was absent and the iron-binding cleft was found in a wide-open conformation, whereas in the previously determined structure of iron-saturated C-lobe of bovine lactoferrin, the iron atom was present and the iron-binding site was in the closed confirmation. STRUCTURED DIGITAL ABSTRACT: trypsin cleaves lactoferrin by enzymatic study ( View interaction).

-	~~==Function==~~	+	Structure of the iron-free true C-terminal half of bovine lactoferrin produced by tryptic digestion and its functional significance in the gut.,Rastogi N, Singh A, Pandey SN, Sinha M, Bhushan A, Kaur P, Sharma S, Singh TP FEBS J. 2014 Jun;281(12):2871-82. doi: 10.1111/febs.12827. Epub 2014 May 16. PMID:24798798<ref>PMID:24798798</ref>
-	~~[[http://www.uniprot.org/uniprot/TRFL_BOVIN TRFL_BOVIN]] Transferrins are~~ iron ~~binding transport proteins which can bind two Fe(3+) ions~~ in ~~association with~~ the ~~binding of an anion~~, ~~usually bicarbonate.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and~~ P.~~aeruginosa.<ref>PMID~~:~~8980754</ref> <ref>PMID:15222473</ref> Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram~~-~~positive bacteria~~.~~<ref>PMID~~:~~8980754<~~/~~ref> <ref>PMID:15222473</ref> The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions~~. ~~This function contributes to the antimicrobial activity~~.~~<ref>~~PMID:~~8980754</ref>~~ <ref>PMID:~~15222473~~</ref>	+

-	~~==About this Structure==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[4oqo]] is~~ a ~~2 chain structure with sequence from [http://en~~.~~wikipedia~~.~~org/wiki/Bos_taurus Bos taurus]~~. ~~Full crystallographic information is available from [http:~~/~~/oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA].~~	+	</div>

-	==~~Reference~~==	+	==See Also==
-	<references ~~group="xtra"~~/><~~references~~/>	+	*[[Lactoferrin\|Lactoferrin]]
		+	== References ==
		+	<references/>
		+	__TOC__
		+	</StructureSection>
	[[Category: Bos taurus]]		[[Category: Bos taurus]]
	[[Category: Bhushan, A.]]		[[Category: Bhushan, A.]]

OCA at 14:04, 12 March 2014

OCA — Wed, 12 Mar 2014 14:04:17 GMT

←Older revision		Revision as of 14:04, 12 March 2014
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-	~~'''Unreleased~~ structure~~'''~~	+	{{STRUCTURE_4oqo\| PDB=4oqo \| SCENE= }}
		+	===Crystal structure of the tryptic generated iron-free C-lobe of bovine Lactoferrin at 2.42 Angstrom resolution===

-	The ~~entry 4oqo~~ is ~~ON HOLD~~	+	==Function==
		+	[[http://www.uniprot.org/uniprot/TRFL_BOVIN TRFL_BOVIN]] Transferrins are iron binding transport proteins which can bind two Fe(3+) ions in association with the binding of an anion, usually bicarbonate.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactotransferrin has antimicrobial activity. The most effective inhibitory activity was seen against E.coli and P.aeruginosa.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> Lactoferricin B is an antimicrobial peptide. Inhibits the growth of Gram-negative and Gram-positive bacteria.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref> The lactotransferrin transferrin-like domain 1 functions as a serine protease of the peptidase S60 family that cuts arginine rich regions. This function contributes to the antimicrobial activity.<ref>PMID:8980754</ref> <ref>PMID:15222473</ref>

-	~~Authors~~: ~~Singh, A~~.~~, Rastogi, N~~.~~, Pandey, S~~.~~, Bhushan, A., Sinha, M., Kaur, P~~.~~, Sharma, S~~.~~, Singh, T~~.P.	+	==About this Structure==
		+	[[4oqo]] is a 2 chain structure with sequence from [http://en.wikipedia.org/wiki/Bos_taurus Bos taurus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=4OQO OCA].

-	~~Description~~: ~~Crystal structure of the tryptic generated iron-free~~ C-lobe ~~of bovine Lactoferrin at 2.42 Angstrom resolution~~	+	==Reference==
		+	<references group="xtra"/><references/>
		+	[[Category: Bos taurus]]
		+	[[Category: Bhushan, A.]]
		+	[[Category: Kaur, P.]]
		+	[[Category: Pandey, S.]]
		+	[[Category: Rastogi, N.]]
		+	[[Category: Sharma, S.]]
		+	[[Category: Singh, A.]]
		+	[[Category: Singh, T P.]]
		+	[[Category: Sinha, M.]]
		+	[[Category: C-lobe]]
		+	[[Category: Hydrolase]]

OCA at 16:49, 3 March 2014

OCA — Mon, 03 Mar 2014 16:49:07 GMT

←Older revision		Revision as of 16:49, 3 March 2014
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	The entry 4oqo is ON HOLD		The entry 4oqo is ON HOLD

-	Authors: Singh, A., Rastogi, N., Pandey, S., Sinha, M., Kaur, P., Sharma, S., Singh, T.P.	+	Authors: Singh, A., Rastogi, N., Pandey, S., Bhushan, A., Sinha, M., Kaur, P., Sharma, S., Singh, T.P.

	Description: Crystal structure of the tryptic generated iron-free C-lobe of bovine Lactoferrin at 2.42 Angstrom resolution		Description: Crystal structure of the tryptic generated iron-free C-lobe of bovine Lactoferrin at 2.42 Angstrom resolution

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

OCA — Wed, 19 Feb 2014 16:19:42 GMT

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

←Older revision

Revision as of 16:19, 19 February 2014