1odq - Revision history

OCA at 18:53, 29 November 2023

OCA — Wed, 29 Nov 2023 18:53:59 GMT

←Older revision		Revision as of 18:53, 29 November 2023
Line 1:		Line 1:

	==PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40==		==PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40==
-	<StructureSection load='1odq' size='340' side='right'caption='[[1odq~~]], [[NMR_Ensembles_of_Models \| 5 NMR models~~]]' scene=''>	+	<StructureSection load='1odq' size='340' side='right'caption='[[1odq]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/~~Human Human~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>
-	</td></tr><tr id='~~related~~'><td class="sblockLbl"><b>[[~~Related_structure~~\|~~Related~~:]]</b></td><td class="sblockDat"~~><div style~~=~~'overflow: auto; max-height: 3em;'>[[1odp\|1odp]], [[1odr\|1odr]]</div~~></td></tr>	+	</td></tr><tr id='method'><td class="sblockLbl"><b>[[Empirical_models\|Method:]]</b></td><td class="sblockDat" id="methodDat">Solution NMR</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=1odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odq OCA], [https://pdbe.org/1odq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1odq RCSB], [https://www.ebi.ac.uk/pdbsum/1odq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1odq 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=1odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odq OCA], [https://pdbe.org/1odq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1odq RCSB], [https://www.ebi.ac.uk/pdbsum/1odq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1odq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[https://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Defects in APOA1 are a cause of high density lipoprotein deficiency type 2 (HDLD2) [MIM:[https://omim.org/entry/604091 604091]]; also known as familial hypoalphalipoproteinemia (FHA). Inheritance is autosomal dominant.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> Defects in APOA1 are a cause of the low HDL levels observed in high density lipoprotein deficiency type 1 (HDLD1) [MIM:[https://omim.org/entry/205400 205400]]; also known as analphalipoproteinemia or Tangier disease (TGD). HDLD1 is a recessive disorder characterized by the absence of plasma HDL, accumulation of cholesteryl esters, premature coronary artery disease, hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting and weakness. In HDLD1 patients, ApoA-I fails to associate with HDL probably because of the faulty conversion of pro-ApoA-I molecules into mature chains, either due to a defect in the converting enzyme activity or a specific structural defect in Tangier ApoA-I.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> Note=A mutation in APOA1 is the cause of amyloid polyneuropathy-nephropathy Iowa type (AMYLIOWA); also known as amyloidosis van Allen type or familial amyloid polyneuropathy type III. AMYLIOWA is a hereditary generalized amyloidosis due to deposition of amyloid mainly constituted by apolipoprotein A1. The clinical picture is dominated by neuropathy in the early stages of the disease and nephropathy late in the course. Death is due in most cases to renal amyloidosis. Severe peptic ulcer disease can occurr in some and hearing loss is frequent. Cataracts is present in several, but vitreous opacities are not observed.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> <ref>PMID:3142462</ref> <ref>PMID:2123470</ref> Defects in APOA1 are a cause of amyloidosis type 8 (AMYL8) [MIM:[https://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> <ref>PMID:1502149</ref>	+	[https://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN] Defects in APOA1 are a cause of high density lipoprotein deficiency type 2 (HDLD2) [MIM:[https://omim.org/entry/604091 604091]; also known as familial hypoalphalipoproteinemia (FHA). Inheritance is autosomal dominant.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> Defects in APOA1 are a cause of the low HDL levels observed in high density lipoprotein deficiency type 1 (HDLD1) [MIM:[https://omim.org/entry/205400 205400]; also known as analphalipoproteinemia or Tangier disease (TGD). HDLD1 is a recessive disorder characterized by the absence of plasma HDL, accumulation of cholesteryl esters, premature coronary artery disease, hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting and weakness. In HDLD1 patients, ApoA-I fails to associate with HDL probably because of the faulty conversion of pro-ApoA-I molecules into mature chains, either due to a defect in the converting enzyme activity or a specific structural defect in Tangier ApoA-I.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> Note=A mutation in APOA1 is the cause of amyloid polyneuropathy-nephropathy Iowa type (AMYLIOWA); also known as amyloidosis van Allen type or familial amyloid polyneuropathy type III. AMYLIOWA is a hereditary generalized amyloidosis due to deposition of amyloid mainly constituted by apolipoprotein A1. The clinical picture is dominated by neuropathy in the early stages of the disease and nephropathy late in the course. Death is due in most cases to renal amyloidosis. Severe peptic ulcer disease can occurr in some and hearing loss is frequent. Cataracts is present in several, but vitreous opacities are not observed.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> <ref>PMID:3142462</ref> <ref>PMID:2123470</ref> Defects in APOA1 are a cause of amyloidosis type 8 (AMYL8) [MIM:[https://omim.org/entry/105200 105200]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> <ref>PMID:1502149</ref>
	== Function ==		== Function ==
-	[[https://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.<ref>PMID:1909888</ref>	+	[https://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN] Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.<ref>PMID:1909888</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
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	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Human~~]]	+	[[Category: Homo sapiens]]
	[[Category: Large Structures]]		[[Category: Large Structures]]
-	[[Category: Cushley~~, R J~~]]	+	[[Category: Cushley RJ]]
-	[[Category: Treleaven~~, W D~~]]	+	[[Category: Treleaven WD]]
-	[[Category: Wang, G]]	+	[[Category: Wang G]]
-	~~[[Category: Apolipoprotein a-i]]~~	+
-	~~[[Category: Cofactor for lcat activation]]~~	+
-	~~[[Category: Lipid transport~~]]	+

OCA at 09:57, 12 May 2021

OCA — Wed, 12 May 2021 09:57:04 GMT

←Older revision		Revision as of 09:57, 12 May 2021
Line 3:		Line 3:
	<StructureSection load='1odq' size='340' side='right'caption='[[1odq]], [[NMR_Ensembles_of_Models \| 5 NMR models]]' scene=''>		<StructureSection load='1odq' size='340' side='right'caption='[[1odq]], [[NMR_Ensembles_of_Models \| 5 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [~~http~~://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [https://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>
-	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1odp\|1odp]], [[1odr\|1odr]]</td></tr>	+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1odp\|1odp]], [[1odr\|1odr]]</div></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=1odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odq OCA], [~~http~~://pdbe.org/1odq PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=1odq RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/1odq PDBsum], [~~http~~://prosat.h-its.org/prosat/prosatexe?pdbcode=1odq 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=1odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odq OCA], [https://pdbe.org/1odq PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=1odq RCSB], [https://www.ebi.ac.uk/pdbsum/1odq PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=1odq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
-	[[~~http~~://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Defects in APOA1 are a cause of high density lipoprotein deficiency type 2 (HDLD2) [MIM:[~~http~~://omim.org/entry/604091 604091]]; also known as familial hypoalphalipoproteinemia (FHA). Inheritance is autosomal dominant.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> Defects in APOA1 are a cause of the low HDL levels observed in high density lipoprotein deficiency type 1 (HDLD1) [MIM:[~~http~~://omim.org/entry/205400 205400]]; also known as analphalipoproteinemia or Tangier disease (TGD). HDLD1 is a recessive disorder characterized by the absence of plasma HDL, accumulation of cholesteryl esters, premature coronary artery disease, hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting and weakness. In HDLD1 patients, ApoA-I fails to associate with HDL probably because of the faulty conversion of pro-ApoA-I molecules into mature chains, either due to a defect in the converting enzyme activity or a specific structural defect in Tangier ApoA-I.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> Note=A mutation in APOA1 is the cause of amyloid polyneuropathy-nephropathy Iowa type (AMYLIOWA); also known as amyloidosis van Allen type or familial amyloid polyneuropathy type III. AMYLIOWA is a hereditary generalized amyloidosis due to deposition of amyloid mainly constituted by apolipoprotein A1. The clinical picture is dominated by neuropathy in the early stages of the disease and nephropathy late in the course. Death is due in most cases to renal amyloidosis. Severe peptic ulcer disease can occurr in some and hearing loss is frequent. Cataracts is present in several, but vitreous opacities are not observed.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> <ref>PMID:3142462</ref> <ref>PMID:2123470</ref> Defects in APOA1 are a cause of amyloidosis type 8 (AMYL8) [MIM:[~~http~~://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> <ref>PMID:1502149</ref>	+	[[https://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Defects in APOA1 are a cause of high density lipoprotein deficiency type 2 (HDLD2) [MIM:[https://omim.org/entry/604091 604091]]; also known as familial hypoalphalipoproteinemia (FHA). Inheritance is autosomal dominant.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> Defects in APOA1 are a cause of the low HDL levels observed in high density lipoprotein deficiency type 1 (HDLD1) [MIM:[https://omim.org/entry/205400 205400]]; also known as analphalipoproteinemia or Tangier disease (TGD). HDLD1 is a recessive disorder characterized by the absence of plasma HDL, accumulation of cholesteryl esters, premature coronary artery disease, hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting and weakness. In HDLD1 patients, ApoA-I fails to associate with HDL probably because of the faulty conversion of pro-ApoA-I molecules into mature chains, either due to a defect in the converting enzyme activity or a specific structural defect in Tangier ApoA-I.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> Note=A mutation in APOA1 is the cause of amyloid polyneuropathy-nephropathy Iowa type (AMYLIOWA); also known as amyloidosis van Allen type or familial amyloid polyneuropathy type III. AMYLIOWA is a hereditary generalized amyloidosis due to deposition of amyloid mainly constituted by apolipoprotein A1. The clinical picture is dominated by neuropathy in the early stages of the disease and nephropathy late in the course. Death is due in most cases to renal amyloidosis. Severe peptic ulcer disease can occurr in some and hearing loss is frequent. Cataracts is present in several, but vitreous opacities are not observed.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> <ref>PMID:3142462</ref> <ref>PMID:2123470</ref> Defects in APOA1 are a cause of amyloidosis type 8 (AMYL8) [MIM:[https://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> <ref>PMID:1502149</ref>
	== Function ==		== Function ==
-	[[~~http~~://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.<ref>PMID:1909888</ref>	+	[[https://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.<ref>PMID:1909888</ref>
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 07:03, 7 August 2019

OCA — Wed, 07 Aug 2019 07:03:36 GMT

←Older revision		Revision as of 07:03, 7 August 2019
Line 1:		Line 1:

	==PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40==		==PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40==
-	<StructureSection load='1odq' size='340' side='right' caption='[[1odq]], [[NMR_Ensembles_of_Models \| 5 NMR models]]' scene=''>	+	<StructureSection load='1odq' size='340' side='right'caption='[[1odq]], [[NMR_Ensembles_of_Models \| 5 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>
Line 25:		Line 25:
	</StructureSection>		</StructureSection>
	[[Category: Human]]		[[Category: Human]]
		+	[[Category: Large Structures]]
	[[Category: Cushley, R J]]		[[Category: Cushley, R J]]
	[[Category: Treleaven, W D]]		[[Category: Treleaven, W D]]

OCA at 09:47, 1 November 2017

OCA — Wed, 01 Nov 2017 09:47:46 GMT

←Older revision		Revision as of 09:47, 1 November 2017
Line 1:		Line 1:
		+
	==PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40==		==PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40==
	<StructureSection load='1odq' size='340' side='right' caption='[[1odq]], [[NMR_Ensembles_of_Models \| 5 NMR models]]' scene=''>		<StructureSection load='1odq' size='340' side='right' caption='[[1odq]], [[NMR_Ensembles_of_Models \| 5 NMR models]]' scene=''>
Line 4:		Line 5:
	<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>		<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1odp\|1odp]], [[1odr\|1odr]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1odp\|1odp]], [[1odr\|1odr]]</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=1odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odq OCA], [http://pdbe.org/1odq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1odq RCSB], [http://www.ebi.ac.uk/pdbsum/1odq 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=1odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odq OCA], [http://pdbe.org/1odq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1odq RCSB], [http://www.ebi.ac.uk/pdbsum/1odq PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1odq ProSAT]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==

OCA at 01:52, 10 September 2015

OCA — Thu, 10 Sep 2015 01:52:43 GMT

←Older revision		Revision as of 01:52, 10 September 2015
Line 2:		Line 2:
	<StructureSection load='1odq' size='340' side='right' caption='[[1odq]], [[NMR_Ensembles_of_Models \| 5 NMR models]]' scene=''>		<StructureSection load='1odq' size='340' side='right' caption='[[1odq]], [[NMR_Ensembles_of_Models \| 5 NMR models]]' scene=''>
	== Structural highlights ==		== Structural highlights ==
-	<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/~~Homo_sapiens Homo sapiens~~]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>	+	<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Human Human]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>
	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1odp\|1odp]], [[1odr\|1odr]]</td></tr>		</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1odp\|1odp]], [[1odr\|1odr]]</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=1odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1odq RCSB], [http://www.ebi.ac.uk/pdbsum/1odq 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=1odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odq OCA], [http://pdbe.org/1odq PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1odq RCSB], [http://www.ebi.ac.uk/pdbsum/1odq PDBsum]</span></td></tr>
	</table>		</table>
	== Disease ==		== Disease ==
Line 18:		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 1odq" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
-	[[Category: ~~Homo sapiens~~]]	+	[[Category: Human]]
	[[Category: Cushley, R J]]		[[Category: Cushley, R J]]
	[[Category: Treleaven, W D]]		[[Category: Treleaven, W D]]

OCA at 12:26, 18 December 2014

OCA — Thu, 18 Dec 2014 12:26:54 GMT

←Older revision		Revision as of 12:26, 18 December 2014
Line 1:		Line 1:
-	~~{{STRUCTURE_1odq\| PDB=1odq \| SCENE= }}~~	+	==PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40==
-	===PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40===	+	<StructureSection load='1odq' size='340' side='right' caption='[[1odq]], [[NMR_Ensembles_of_Models \| 5 NMR models]]' scene=''>
-	~~{{ABSTRACT_PUBMED_8664326}}~~	+	== Structural highlights ==
		+	<table><tr><td colspan='2'>[[1odq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1ODQ FirstGlance]. <br>
		+	</td></tr><tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1odp\|1odp]], [[1odr\|1odr]]</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=1odq FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1odq OCA], [http://www.rcsb.org/pdb/explore.do?structureId=1odq RCSB], [http://www.ebi.ac.uk/pdbsum/1odq PDBsum]</span></td></tr>
		+	</table>
		+	== Disease ==
		+	[[http://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Defects in APOA1 are a cause of high density lipoprotein deficiency type 2 (HDLD2) [MIM:[http://omim.org/entry/604091 604091]]; also known as familial hypoalphalipoproteinemia (FHA). Inheritance is autosomal dominant.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> Defects in APOA1 are a cause of the low HDL levels observed in high density lipoprotein deficiency type 1 (HDLD1) [MIM:[http://omim.org/entry/205400 205400]]; also known as analphalipoproteinemia or Tangier disease (TGD). HDLD1 is a recessive disorder characterized by the absence of plasma HDL, accumulation of cholesteryl esters, premature coronary artery disease, hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting and weakness. In HDLD1 patients, ApoA-I fails to associate with HDL probably because of the faulty conversion of pro-ApoA-I molecules into mature chains, either due to a defect in the converting enzyme activity or a specific structural defect in Tangier ApoA-I.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> Note=A mutation in APOA1 is the cause of amyloid polyneuropathy-nephropathy Iowa type (AMYLIOWA); also known as amyloidosis van Allen type or familial amyloid polyneuropathy type III. AMYLIOWA is a hereditary generalized amyloidosis due to deposition of amyloid mainly constituted by apolipoprotein A1. The clinical picture is dominated by neuropathy in the early stages of the disease and nephropathy late in the course. Death is due in most cases to renal amyloidosis. Severe peptic ulcer disease can occurr in some and hearing loss is frequent. Cataracts is present in several, but vitreous opacities are not observed.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> <ref>PMID:3142462</ref> <ref>PMID:2123470</ref> Defects in APOA1 are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8240372</ref> <ref>PMID:8282791</ref> <ref>PMID:1502149</ref>
		+	== Function ==
		+	[[http://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.<ref>PMID:1909888</ref>
		+	<div style="background-color:#fffaf0;">
		+	== Publication Abstract from PubMed ==
		+	The segment, YSDELRQRLAARLEALKENG, corresponding to residues 166 to 185 of human serum apolipoprotein A-I, was studied by circular dichroism and NMR spectroscopy in sodium dodecyl sulfate and dodecylphosphocholine micelles. 2-Dimensional NOESY, TOCSY and DQF-COSY spectra of apoA-I(166-185) in perdeuterated sodium dodecyl sulfate (SDS-d25) and dodecylphosphocholine (DPC-d38) micelles were collected at a peptide/SDS (DPC) ratio of 1:40. Similar CD spectra and NOE connectivity patterns were observed for apoA-I(166-185) in SDS and DPC, indicating a similar helical conformation in both. Conformations of apoA-I(166-185) in DPC-d38 micelles, and in SDS-d25 micelles at two pH values, 6.6 and 3.7, were determined using distance geometry calculations. Backbone superposition (N,C alpha,C = O) for an ensemble of twenty-nine structures in DPC at pH 6.0 gave a RMSD of 0.45 +/- 0.09 A for the region D168 to K182, while for all atoms it was 1.60 +/- 0.17 A. In SDS, the ensemble of nineteen structures each at pH 6.6 and 3.7 gave RMSDs of 0.28 +/- 0.07 A and 0.35 +/- 0.10 A, respectively, for the region D168 to K182. RMSD for superposition of all atoms was 1.36 +/- 0.10 A and 1.38 +/- 0.21 A at the respective pH values. In all cases a highly defined class A amphipathic helical structure was found for the region R171 to K182. Since the same structure occurs in micelles with either negatively charged or zwitterionic head groups it strongly suggests a dominant role for hydrophobic interactions in stabilizing the complex. The Y166 aromatic ring is bent back upon the helix axis at the lower pH. NMR determination of pKa values for D168, E169, E179 and E183 in the presence of SDS or DPC indicated a micro-pH at the micellar surface approximately one pH unit higher than the normal residue pKa. SDS interactions with the peptide were examined by collecting 1H NOESY spectra in the presence of protiated SDS. Residues R171, R173, R177, as well as the aromatic ring of Y166, were shown by intermolecular NOE measurements to interact with SDS, hence a key interaction in stabilizing the complex appears to be between interfacial basic side-chains and SDS alkyl chains.

-	~~==Disease==~~	+	Conformation of human serum apolipoprotein A-I(166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence for specific peptide-SDS interactions.,Wang G, Treleaven WD, Cushley RJ Biochim Biophys Acta. 1996 Jun 11;1301(3):174-84. PMID:8664326<ref>PMID:8664326</ref>
-	~~[[http://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Defects in APOA1 are a cause~~ of ~~high density lipoprotein deficiency type 2~~ (~~HDLD2~~) ~~[MIM:[http://omim.org/entry/604091 604091]]; also known as familial hypoalphalipoproteinemia (FHA). Inheritance is autosomal dominant.<ref>PMID:8240372</ref><ref>PMID:8282791</ref> Defects~~ in ~~APOA1 are a cause~~ of ~~the low HDL levels observed in high density lipoprotein deficiency type 1 (HDLD1) [MIM:[http://omim.org/entry/205400 205400]]; also known as analphalipoproteinemia~~ or ~~Tangier disease (TGD). HDLD1 is a recessive disorder characterized~~ by ~~the absence of plasma HDL, accumulation of cholesteryl esters, premature coronary artery disease, hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting~~ and ~~weakness~~. In HDLD1 patients, ApoA-I fails to associate with HDL probably because of the faulty conversion of pro-ApoA-I molecules into mature chains, either due to a defect in the converting enzyme activity or a specific ~~structural defect in Tangier ApoA~~-I.<ref>PMID:8240372</ref><ref>PMID:8282791</ref> Note=A mutation in APOA1 is the cause of amyloid polyneuropathy-nephropathy Iowa type (AMYLIOWA); also known as amyloidosis van Allen type or familial amyloid polyneuropathy type III. AMYLIOWA is a hereditary generalized amyloidosis due to deposition of amyloid mainly constituted by apolipoprotein A1. The clinical picture is dominated by neuropathy in the early stages of the disease and nephropathy late in the course. Death is due in most cases to renal amyloidosis. Severe peptic ulcer disease can occurr in some and hearing loss is frequent. Cataracts is present in several, ~~but vitreous opacities are not observed~~.~~<ref>PMID:8240372</ref><ref>PMID:8282791</ref><ref>PMID:3142462</ref><ref>PMID:2123470</ref> Defects in APOA1 are a cause of amyloidosis type 8~~ (~~AMYL8~~) ~~[MIM~~:~~[http://omim.org/entry/105200 105200]]; also known as systemic non~~-~~neuropathic amyloidosis or Ostertag-type amyloidosis~~. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:~~8240372</ref><ref>PMID:8282791</ref>~~<ref>PMID:~~1502149~~</ref>	+

-	~~==Function==~~	+	From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
-	~~[[http:~~/~~/www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Participates in the reverse transport~~ of ~~cholesterol from tissues to~~ the ~~liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT)~~. ~~As part~~ of ~~the SPAP complex, activates spermatozoa motility~~.<~~ref~~>~~PMID:1909888~~</~~ref~~>	+	</div>
-		+	== References ==
-	==~~About this Structure==~~	+	<references/>
-	[[1odq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA].	+	__TOC__
-		+	</StructureSection>
-	~~==Reference~~==	+
-	~~<ref group="xtra">PMID:008664326</ref>~~<references ~~group="xtra"~~/><~~references~~/>	+
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Cushley, R J.]]	+	[[Category: Cushley, R J]]
-	[[Category: Treleaven, W D.]]	+	[[Category: Treleaven, W D]]
-	[[Category: Wang, G.]]	+	[[Category: Wang, G]]
	[[Category: Apolipoprotein a-i]]		[[Category: Apolipoprotein a-i]]
	[[Category: Cofactor for lcat activation]]		[[Category: Cofactor for lcat activation]]
	[[Category: Lipid transport]]		[[Category: Lipid transport]]

OCA at 19:58, 24 March 2013

OCA — Sun, 24 Mar 2013 19:58:31 GMT

←Older revision		Revision as of 19:58, 24 March 2013
Line 1:		Line 1:
-	[[Image:1odq.png\|left\|200px]]
-
	{{STRUCTURE_1odq\| PDB=1odq \| SCENE= }}		{{STRUCTURE_1odq\| PDB=1odq \| SCENE= }}
-
	===PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40===		===PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40===
		+	{{ABSTRACT_PUBMED_8664326}}

-	~~{{ABSTRACT_PUBMED_8664326}}~~	+	==Disease==
		+	[[http://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Defects in APOA1 are a cause of high density lipoprotein deficiency type 2 (HDLD2) [MIM:[http://omim.org/entry/604091 604091]]; also known as familial hypoalphalipoproteinemia (FHA). Inheritance is autosomal dominant.<ref>PMID:8240372</ref><ref>PMID:8282791</ref> Defects in APOA1 are a cause of the low HDL levels observed in high density lipoprotein deficiency type 1 (HDLD1) [MIM:[http://omim.org/entry/205400 205400]]; also known as analphalipoproteinemia or Tangier disease (TGD). HDLD1 is a recessive disorder characterized by the absence of plasma HDL, accumulation of cholesteryl esters, premature coronary artery disease, hepatosplenomegaly, recurrent peripheral neuropathy and progressive muscle wasting and weakness. In HDLD1 patients, ApoA-I fails to associate with HDL probably because of the faulty conversion of pro-ApoA-I molecules into mature chains, either due to a defect in the converting enzyme activity or a specific structural defect in Tangier ApoA-I.<ref>PMID:8240372</ref><ref>PMID:8282791</ref> Note=A mutation in APOA1 is the cause of amyloid polyneuropathy-nephropathy Iowa type (AMYLIOWA); also known as amyloidosis van Allen type or familial amyloid polyneuropathy type III. AMYLIOWA is a hereditary generalized amyloidosis due to deposition of amyloid mainly constituted by apolipoprotein A1. The clinical picture is dominated by neuropathy in the early stages of the disease and nephropathy late in the course. Death is due in most cases to renal amyloidosis. Severe peptic ulcer disease can occurr in some and hearing loss is frequent. Cataracts is present in several, but vitreous opacities are not observed.<ref>PMID:8240372</ref><ref>PMID:8282791</ref><ref>PMID:3142462</ref><ref>PMID:2123470</ref> Defects in APOA1 are a cause of amyloidosis type 8 (AMYL8) [MIM:[http://omim.org/entry/105200 105200]]; also known as systemic non-neuropathic amyloidosis or Ostertag-type amyloidosis. AMYL8 is a hereditary generalized amyloidosis due to deposition of apolipoprotein A1, fibrinogen and lysozyme amyloids. Viscera are particularly affected. There is no involvement of the nervous system. Clinical features include renal amyloidosis resulting in nephrotic syndrome, arterial hypertension, hepatosplenomegaly, cholestasis, petechial skin rash.<ref>PMID:8240372</ref><ref>PMID:8282791</ref><ref>PMID:1502149</ref>
		+
		+	==Function==
		+	[[http://www.uniprot.org/uniprot/APOA1_HUMAN APOA1_HUMAN]] Participates in the reverse transport of cholesterol from tissues to the liver for excretion by promoting cholesterol efflux from tissues and by acting as a cofactor for the lecithin cholesterol acyltransferase (LCAT). As part of the SPAP complex, activates spermatozoa motility.<ref>PMID:1909888</ref>

	==About this Structure==		==About this Structure==
Line 11:		Line 13:

	==Reference==		==Reference==
-	<ref group="xtra">PMID:008664326</ref><references group="xtra"/>	+	<ref group="xtra">PMID:008664326</ref><references group="xtra"/><references/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Cushley, R J.]]		[[Category: Cushley, R J.]]

OCA: Protected "1odq" [edit=sysop:move=sysop]

OCA — Tue, 14 Aug 2012 18:43:03 GMT

Protected "1odq" [edit=sysop:move=sysop]

←Older revision

Revision as of 18:43, 14 August 2012

OCA at 18:43, 14 August 2012

OCA — Tue, 14 Aug 2012 18:43:02 GMT

←Older revision		Revision as of 18:43, 14 August 2012
Line 1:		Line 1:
-	{{Seed}}
	[[Image:1odq.png\|left\|200px]]		[[Image:1odq.png\|left\|200px]]

-	<!--
-	The line below this paragraph, containing "STRUCTURE_1odq", creates the "Structure Box" on the page.
-	You may change the PDB parameter (which sets the PDB file loaded into the applet)
-	or the SCENE parameter (which sets the initial scene displayed when the page is loaded),
-	or leave the SCENE parameter empty for the default display.
-	-->
	{{STRUCTURE_1odq\| PDB=1odq \| SCENE= }}		{{STRUCTURE_1odq\| PDB=1odq \| SCENE= }}

	===PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40===		===PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40===

-
-	<!--
-	The line below this paragraph, {{ABSTRACT_PUBMED_8664326}}, adds the Publication Abstract to the page
-	(as it appears on PubMed at http://www.pubmed.gov), where 8664326 is the PubMed ID number.
-	-->
	{{ABSTRACT_PUBMED_8664326}}		{{ABSTRACT_PUBMED_8664326}}

	==About this Structure==		==About this Structure==
-	~~1ODQ is a~~ [[~~Single protein~~]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA].	+	[[1odq]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA].

	==Reference==		==Reference==
-	Conformation of human serum apolipoprotein A-I(166-185) in the presence of sodium dodecyl sulfate or dodecylphosphocholine by 1H-NMR and CD. Evidence for specific peptide-SDS interactions., Wang G, Treleaven WD, Cushley RJ, Biochim Biophys Acta. 1996 Jun 11;1301(3):174-84. PMID:~~[http://www.ncbi.nlm.nih.gov~~/~~pubmed~~/~~8664326 8664326]~~	+	<ref group="xtra">PMID:008664326</ref><references group="xtra"/>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
-	[[Category: Single protein]]
	[[Category: Cushley, R J.]]		[[Category: Cushley, R J.]]
	[[Category: Treleaven, W D.]]		[[Category: Treleaven, W D.]]
Line 32:		Line 19:
	[[Category: Cofactor for lcat activation]]		[[Category: Cofactor for lcat activation]]
	[[Category: Lipid transport]]		[[Category: Lipid transport]]
-
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:39:49 2008''

OCA at 13:39, 27 July 2008

OCA — Sun, 27 Jul 2008 13:39:52 GMT

←Older revision		Revision as of 13:39, 27 July 2008
Line 1:		Line 1:
-	[[Image:1odq.~~jpg~~\|left\|200px]]	+	{{Seed}}
		+	[[Image:1odq.png\|left\|200px]]

	<!--		<!--
Line 9:		Line 10:
	{{STRUCTURE_1odq\| PDB=1odq \| SCENE= }}		{{STRUCTURE_1odq\| PDB=1odq \| SCENE= }}

-	~~'''~~PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40~~'''~~	+	===PEPTIDE OF HUMAN APOA-I RESIDUES 166-185. NMR, 5 STRUCTURES AT PH 3.7, 37 DEGREES CELSIUS AND PEPTIDE:SDS MOLE RATIO OF 1:40===


-	~~==Overview==~~	+	<!--
-	The ~~segment~~, ~~YSDELRQRLAARLEALKENG~~, ~~corresponding~~ to residues 166 to 185 of human serum apolipoprotein A-I, was studied by circular dichroism and NMR spectroscopy in sodium dodecyl sulfate and dodecylphosphocholine micelles. 2-Dimensional NOESY, TOCSY and DQF-COSY spectra of apoA-I(~~166-185) in perdeuterated sodium dodecyl sulfate (SDS-d25) and dodecylphosphocholine (DPC-d38) micelles were collected~~ at ~~a peptide/SDS (DPC) ratio of 1~~:40. Similar CD spectra and NOE connectivity patterns were observed for apoA-I(166-185) in SDS and DPC, indicating a similar helical conformation in both. Conformations of apoA-I(166-185) in DPC-d38 micelles, and in SDS-d25 micelles at two pH values, 6.6 and 3.7, were determined using distance geometry calculations. Backbone superposition (N,C alpha,C = O) for an ensemble of twenty-nine structures in DPC at pH 6.0 gave a RMSD of 0.45 +/~~- 0.09 A for the region D168 to K182, while for all atoms it was 1.60 +~~/~~- 0~~.~~17 A~~. ~~In SDS~~, the ensemble of nineteen structures each at pH 6.6 and 3.7 gave RMSDs of 0.28 +/- 0.07 A and 0.35 +/- 0.10 A, respectively, for the region D168 to K182. RMSD for superposition of all atoms was 1.36 +/- 0.10 A and 1.38 +/- 0.21 A at the respective pH values. In all cases a highly defined class A amphipathic helical structure was found for the region R171 to K182. Since the same structure occurs in micelles with either negatively charged or zwitterionic head groups it strongly suggests a dominant role for hydrophobic interactions in stabilizing the complex. The Y166 aromatic ring is ~~bent back upon~~ the ~~helix axis at the lower pH~~. ~~NMR determination of pKa values for D168, E169, E179 and E183 in the presence of SDS or DPC indicated a micro~~-pH at the micellar surface approximately one pH unit higher than the normal residue pKa. SDS interactions with the peptide were examined by collecting 1H NOESY spectra in the presence of protiated SDS. Residues R171, R173, R177, as well as the aromatic ring of Y166, were shown by intermolecular NOE measurements to interact with SDS, hence a key interaction in stabilizing the complex appears to be between interfacial basic side-~~chains and SDS alkyl chains.~~	+	The line below this paragraph, {{ABSTRACT_PUBMED_8664326}}, adds the Publication Abstract to the page
		+	(as it appears on PubMed at http://www.pubmed.gov), where 8664326 is the PubMed ID number.
		+	-->
		+	{{ABSTRACT_PUBMED_8664326}}

	==About this Structure==		==About this Structure==
-	1ODQ 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=1ODQ OCA].	+	1ODQ is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens]. Full experimental information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1ODQ OCA].

	==Reference==		==Reference==
Line 28:		Line 32:
	[[Category: Cofactor for lcat activation]]		[[Category: Cofactor for lcat activation]]
	[[Category: Lipid transport]]		[[Category: Lipid transport]]
-	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on ~~Sat May 3 03~~:43:00 2008''	+
		+	''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 16:39:49 2008''