4e52 - Revision history

OCA at 02:49, 21 November 2024

2024-11-21T02:49:08Z

@@ Line 10: / Line 10: @@
 == Function ==
 [https://www.uniprot.org/uniprot/SFTPD_HUMAN SFTPD_HUMAN] Contributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
 __TOC__
 </StructureSection>

OCA at 14:52, 14 March 2024

2024-03-14T14:52:42Z

← Older revision		Revision as of 14:52, 14 March 2024
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	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e52]] is a 3 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=4E52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E52 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e52]] is a 3 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=4E52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E52 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GMH:L-GLYCERO-D-MANNO-HEPTOPYRANOSE'>GMH</scene>, <scene name='pdbligand=KD5:4,7-ANHYDRO-3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KD5</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]] 1.7Å</td></tr>
			<tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GMH:L-GLYCERO-D-MANNO-HEPTOPYRANOSE'>GMH</scene>, <scene name='pdbligand=KD5:4,7-ANHYDRO-3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KD5</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=4e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e52 OCA], [https://pdbe.org/4e52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e52 RCSB], [https://www.ebi.ac.uk/pdbsum/4e52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e52 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=4e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e52 OCA], [https://pdbe.org/4e52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e52 RCSB], [https://www.ebi.ac.uk/pdbsum/4e52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e52 ProSAT]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[https://www.uniprot.org/uniprot/SFTPD_HUMAN SFTPD_HUMAN]] Contributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.		[https://www.uniprot.org/uniprot/SFTPD_HUMAN SFTPD_HUMAN] Contributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
	~~<div style="background-color:#fffaf0;">~~
	~~== Publication Abstract from PubMed ==~~
	The carbohydrate recognition domains (CRDs) of lung collectin surfactant protein D (SP-D) recognize sugar patterns on the surface of lung pathogens and promote phagocytosis. Using Haemophilus influenzae Eagan strains expressing well-characterized lipopolysaccharide (LPS) surface structures of various levels of complexity, we show that bacterial recognition and binding by SP-D is inversely related to LPS chain extent and complexity. The crystal structure of a biologically active recombinant trimeric SP-D CRD complexed with a delipidated Eagan 4A LPS suggests that efficient LPS recognition by SP-D requires multiple binding interactions utilizing the three major ligand-binding determinants in the SP-D binding pocket, with Ca-dependent binding of inner-core heptose accompanied by interaction of anhydro-Kdo (4,7-anhydro-3-deoxy-d-manno-oct-2-ulosonic acid) with Arg343 and Asp325. Combined with enzyme-linked immunosorbent assays (ELISAs) and fluorescence-activated cell sorter (FACS) binding analyses, our results show that extended LPS structures previously thought to be targets for collectins are important in shielding the more vulnerable sites in the LPS core, revealing a mechanism by which pathogens with complex LPS extensions efficiently evade a first-line mucosal innate immune defense. The structure also reveals for the first time the dominant form of anhydro-Kdo.

	Crystal Structure of a Complex of Surfactant Protein D (SP-D) and Haemophilus influenzae Lipopolysaccharide Reveals Shielding of Core Structures in SP-D-Resistant Strains.,Clark HW, Mackay RM, Deadman ME, Hood DW, Madsen J, Moxon ER, Townsend JP, Reid KB, Ahmed A, Shaw AJ, Greenhough TJ, Shrive AK Infect Immun. 2016 Apr 22;84(5):1585-92. doi: 10.1128/IAI.01239-15. Print 2016, May. PMID:26953329<ref>PMID:26953329</ref>

	~~From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>~~
	~~</div>~~
	~~<div class="pdbe-citations 4e52" style="background-color:#fffaf0;"></div>~~
	~~== References ==~~
	~~<references/>~~
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>

OCA at 06:50, 28 September 2022

2022-09-28T06:50:21Z

← Older revision		Revision as of 06:50, 28 September 2022
Line 1:		Line 1:

	==Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D==		==Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D==
	<StructureSection load='4e52' size='340' side='right' caption='[[4e52]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4e52' size='340' side='right'caption='[[4e52]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e52]] is a 3 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=4E52 OCA]. For a <b>guided tour on the structure components</b> use [~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4E52 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e52]] is a 3 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=4E52 OCA]. For a <b>guided tour on the structure components</b> use [https://proteopedia.org/fgij/fg.htm?mol=4E52 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GMH:L-GLYCERO-D-MANNO-HEPTOPYRANOSE'>GMH</scene>, <scene name='pdbligand=KD5:4,7-ANHYDRO-3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KD5</scene>~~</td></tr>~~		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GMH:L-GLYCERO-D-MANNO-HEPTOPYRANOSE'>GMH</scene>, <scene name='pdbligand=KD5:4,7-ANHYDRO-3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KD5</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pw9\|1pw9]], [[1pwb\|1pwb]], [[3ikn\|3ikn]], [[3ikp\|3ikp]], [[3ikq\|3ikq]], [[3ikr\|3ikr]]</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=4e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e52 OCA], [https://pdbe.org/4e52 PDBe], [https://www.rcsb.org/pdb/explore.do?structureId=4e52 RCSB], [https://www.ebi.ac.uk/pdbsum/4e52 PDBsum], [https://prosat.h-its.org/prosat/prosatexe?pdbcode=4e52 ProSAT]</span></td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SFTPD, COLEC7, PSPD, SFTP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[~~http~~://~~oca~~.~~weizmann.ac.il/oca-docs~~/fgij/fg.htm?mol=4e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e52 OCA], [~~http~~://pdbe.org/4e52 PDBe], [~~http~~://www.rcsb.org/pdb/explore.do?structureId=4e52 RCSB], [~~http~~://www.ebi.ac.uk/pdbsum/4e52 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
	[[~~http~~://www.uniprot.org/uniprot/SFTPD_HUMAN SFTPD_HUMAN]] Contributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.		[[https://www.uniprot.org/uniprot/SFTPD_HUMAN SFTPD_HUMAN]] Contributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
Line 24:		Line 22:
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Human~~]]		[[Category: Homo sapiens]]
	[[Category: ~~Greenhough, T J~~]]		[[Category: Large Structures]]
	[[Category: ~~Shrive, A K~~]]		[[Category: Greenhough TJ]]
	[[Category: ~~Alpha-helical coiled coil]]~~		[[Category: Shrive AK]]
	~~[[Category: Carbohydrate recognition domain]]~~
	~~[[Category: Lectin]]~~
	~~[[Category: Neck+crd]]~~
	~~[[Category: Sugar binding protein]]~~
	~~[[Category: Trimeric recombinant collectin fragment~~]]

OCA at 18:38, 10 May 2016

2016-05-10T18:38:09Z

← Older revision		Revision as of 18:38, 10 May 2016
Line 1:		Line 1:

	==Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D==		==Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D==
	<StructureSection load='4e52' size='340' side='right' caption='[[4e52]], [[Resolution\|resolution]] 1.70Å' scene=''>		<StructureSection load='4e52' size='340' side='right' caption='[[4e52]], [[Resolution\|resolution]] 1.70Å' scene=''>
	== Structural highlights ==		== Structural highlights ==
	<table><tr><td colspan='2'>[[4e52]] is a 3 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=4E52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E52 FirstGlance]. <br>		<table><tr><td colspan='2'>[[4e52]] is a 3 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=4E52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E52 FirstGlance]. <br>
	</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GMH:L-GLYCERO-D-MANNO-HEPTOPYRANOSE'>GMH</scene>, <scene name='pdbligand=KD5:4,7-ANHYDRO-3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KD5</scene></td></tr>		</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GMH:L-GLYCERO-D-MANNO-HEPTOPYRANOSE'>GMH</scene>, <scene name='pdbligand=KD5:4,7-ANHYDRO-3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KD5</scene></td></tr>
	<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pw9\|1pw9]], [[1pwb\|1pwb]], [[3ikn\|3ikn]], [[3ikp\|3ikp]], [[3ikq\|3ikq]], [[3ikr\|3ikr]]</td></tr>		<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pw9\|1pw9]], [[1pwb\|1pwb]], [[3ikn\|3ikn]], [[3ikp\|3ikp]], [[3ikq\|3ikq]], [[3ikr\|3ikr]]</td></tr>
	<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SFTPD, COLEC7, PSPD, SFTP4 ([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">SFTPD, COLEC7, PSPD, SFTP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 HUMAN])</td></tr>
	<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e52 RCSB], [http://www.ebi.ac.uk/pdbsum/4e52 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=4e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e52 OCA], [http://pdbe.org/4e52 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=4e52 RCSB], [http://www.ebi.ac.uk/pdbsum/4e52 PDBsum]</span></td></tr>
	</table>		</table>
	== Function ==		== Function ==
Line 12:		Line 13:
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==
	The ~~crystal structures~~ of ~~a biologically and therapeutically active recombinant homotrimeric fragment of human~~ lung surfactant protein D ~~with a series~~ of ~~bound ligands have been determined~~. ~~While the~~ structures ~~reveal~~ various ~~different binding modes~~, ~~all utilise a similarly positioned pair of mannose-type O3'~~ and ~~O4' hydroxyls with no direct interaction between any non~~-~~terminal sugar~~ and ~~protein~~. The ~~orientation, position, and~~ interactions of the bound terminal sugar depend on the sugar itself, the presence and form of glycosidic linkage, and the environment in the crystal, which, via Asp325, places stereochemical and electronic constraints, different for the three ~~different subunits~~ in the ~~homotrimer~~, ~~on the ligand~~-binding ~~site. As a direct consequence~~ of ~~this influence~~, ~~the other binding~~-~~pocket flanking residue,~~ Arg343~~, exhibits variable conformation~~ and ~~variable interactions~~ with ~~bound ligand~~ and ~~leaves open~~ to ~~question which orientation of terminal mannobiose, and of other terminal disaccharides, may~~ be ~~present~~ in ~~extended physiological ligands~~. The ~~combined structural evidence shows that there is significant flexibility in recognition; that Asp325, in addition to Arg343, is an important determinant~~ of ~~ligand selectivity, recognition, and binding; and that differences in crystal contact interfaces exert, through Asp325, significant influence on preferred binding modes~~.		The carbohydrate recognition domains (CRDs) of lung collectin surfactant protein D (SP-D) recognize sugar patterns on the surface of lung pathogens and promote phagocytosis. Using Haemophilus influenzae Eagan strains expressing well-characterized lipopolysaccharide (LPS) surface structures of various levels of complexity, we show that bacterial recognition and binding by SP-D is inversely related to LPS chain extent and complexity. The crystal structure of a biologically active recombinant trimeric SP-D CRD complexed with a delipidated Eagan 4A LPS suggests that efficient LPS recognition by SP-D requires multiple binding interactions utilizing the three major ligand-binding determinants in the SP-D binding pocket, with Ca-dependent binding of inner-core heptose accompanied by interaction of anhydro-Kdo (4,7-anhydro-3-deoxy-d-manno-oct-2-ulosonic acid) with Arg343 and Asp325. Combined with enzyme-linked immunosorbent assays (ELISAs) and fluorescence-activated cell sorter (FACS) binding analyses, our results show that extended LPS structures previously thought to be targets for collectins are important in shielding the more vulnerable sites in the LPS core, revealing a mechanism by which pathogens with complex LPS extensions efficiently evade a first-line mucosal innate immune defense. The structure also reveals for the first time the dominant form of anhydro-Kdo.

	~~Structural characterisation~~ of ~~ligand~~-~~binding determinants~~ in ~~human lung surfactant protein~~ D~~: influence of Asp325~~.,~~Shrive AK~~, ~~Martin C~~, ~~Burns I~~, ~~Paterson JM~~, ~~Martin JD~~, Townsend JP, ~~Waters P, Clark HW~~, ~~Kishore U~~, ~~Reid KB~~, Greenhough TJ ~~J Mol Biol~~. ~~2009 Dec 11~~;~~394~~(4):~~776~~-88. ~~Epub 2009 Sep 30~~. PMID:~~19799916~~<ref>PMID:~~19799916~~</ref>		Crystal Structure of a Complex of Surfactant Protein D (SP-D) and Haemophilus influenzae Lipopolysaccharide Reveals Shielding of Core Structures in SP-D-Resistant Strains.,Clark HW, Mackay RM, Deadman ME, Hood DW, Madsen J, Moxon ER, Townsend JP, Reid KB, Ahmed A, Shaw AJ, Greenhough TJ, Shrive AK Infect Immun. 2016 Apr 22;84(5):1585-92. doi: 10.1128/IAI.01239-15. Print 2016, May. PMID:26953329<ref>PMID:26953329</ref>

	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 4e52" style="background-color:#fffaf0;"></div>
	== References ==		== References ==
	<references/>		<references/>
	__TOC__		__TOC__
	</StructureSection>		</StructureSection>
	[[Category: ~~Homo sapiens~~]]		[[Category: Human]]
	[[Category: Greenhough, T J]]		[[Category: Greenhough, T J]]
	[[Category: Shrive, A K]]		[[Category: Shrive, A K]]

OCA at 03:26, 25 December 2014

2014-12-25T03:26:32Z

← Older revision		Revision as of 03:26, 25 December 2014
Line 8:		Line 8:
	<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=4e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e52 RCSB], [http://www.ebi.ac.uk/pdbsum/4e52 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=4e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e52 RCSB], [http://www.ebi.ac.uk/pdbsum/4e52 PDBsum]</span></td></tr>
	</table>		</table>
			== Function ==
			[[http://www.uniprot.org/uniprot/SFTPD_HUMAN SFTPD_HUMAN]] Contributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
	<div style="background-color:#fffaf0;">		<div style="background-color:#fffaf0;">
	== Publication Abstract from PubMed ==		== Publication Abstract from PubMed ==

OCA at 11:20, 21 December 2014

2014-12-21T11:20:56Z

← Older revision		Revision as of 11:20, 21 December 2014
Line 1:		Line 1:
	~~{{STRUCTURE_4e52\| PDB=4e52 \| SCENE= }}~~		==Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D==
	===Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D===		<StructureSection load='4e52' size='340' side='right' caption='[[4e52]], [[Resolution\|resolution]] 1.70Å' scene=''>
	~~{{ABSTRACT_PUBMED_19799916}}~~		== Structural highlights ==
			<table><tr><td colspan='2'>[[4e52]] is a 3 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=4E52 OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=4E52 FirstGlance]. <br>
			</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand\|Ligands:]]</b></td><td class="sblockDat"><scene name='pdbligand=CA:CALCIUM+ION'>CA</scene>, <scene name='pdbligand=GMH:L-GLYCERO-D-MANNO-HEPTOPYRANOSE'>GMH</scene>, <scene name='pdbligand=KD5:4,7-ANHYDRO-3-DEOXY-D-MANNO-OCT-2-ULOSONIC+ACID'>KD5</scene></td></tr>
			<tr id='related'><td class="sblockLbl"><b>[[Related_structure\|Related:]]</b></td><td class="sblockDat">[[1pw9\|1pw9]], [[1pwb\|1pwb]], [[3ikn\|3ikn]], [[3ikp\|3ikp]], [[3ikq\|3ikq]], [[3ikr\|3ikr]]</td></tr>
			<tr id='gene'><td class="sblockLbl"><b>[[Gene\|Gene:]]</b></td><td class="sblockDat">SFTPD, COLEC7, PSPD, SFTP4 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=9606 Homo sapiens])</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=4e52 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=4e52 OCA], [http://www.rcsb.org/pdb/explore.do?structureId=4e52 RCSB], [http://www.ebi.ac.uk/pdbsum/4e52 PDBsum]</span></td></tr>
			</table>
			<div style="background-color:#fffaf0;">
			== Publication Abstract from PubMed ==
			The crystal structures of a biologically and therapeutically active recombinant homotrimeric fragment of human lung surfactant protein D with a series of bound ligands have been determined. While the structures reveal various different binding modes, all utilise a similarly positioned pair of mannose-type O3' and O4' hydroxyls with no direct interaction between any non-terminal sugar and protein. The orientation, position, and interactions of the bound terminal sugar depend on the sugar itself, the presence and form of glycosidic linkage, and the environment in the crystal, which, via Asp325, places stereochemical and electronic constraints, different for the three different subunits in the homotrimer, on the ligand-binding site. As a direct consequence of this influence, the other binding-pocket flanking residue, Arg343, exhibits variable conformation and variable interactions with bound ligand and leaves open to question which orientation of terminal mannobiose, and of other terminal disaccharides, may be present in extended physiological ligands. The combined structural evidence shows that there is significant flexibility in recognition; that Asp325, in addition to Arg343, is an important determinant of ligand selectivity, recognition, and binding; and that differences in crystal contact interfaces exert, through Asp325, significant influence on preferred binding modes.

	~~==Function==~~		Structural characterisation of ligand-binding determinants in human lung surfactant protein D: influence of Asp325.,Shrive AK, Martin C, Burns I, Paterson JM, Martin JD, Townsend JP, Waters P, Clark HW, Kishore U, Reid KB, Greenhough TJ J Mol Biol. 2009 Dec 11;394(4):776-88. Epub 2009 Sep 30. PMID:19799916<ref>PMID:19799916</ref>
	~~[[http~~:~~//www~~.~~uniprot~~.~~org/uniprot/SFTPD_HUMAN SFTPD_HUMAN]] Contributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant~~. ~~Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties~~.

	~~==About this Structure==~~		From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br>
	~~[[4e52]] is~~ a ~~3 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=4E52 OCA].~~		</div>
			== References ==
	==~~Reference~~==		<references/>
	~~<ref group="xtra">PMID:019799916</ref><ref group="xtra">PMID:012888356</ref>~~<references ~~group="xtra"~~/><~~references~~/>		__TOC__
			</StructureSection>
	[[Category: Homo sapiens]]		[[Category: Homo sapiens]]
	[[Category: Greenhough, T J.]]		[[Category: Greenhough, T J]]
	[[Category: Shrive, A K.]]		[[Category: Shrive, A K]]
	[[Category: Alpha-helical coiled coil]]		[[Category: Alpha-helical coiled coil]]
	[[Category: Carbohydrate recognition domain]]		[[Category: Carbohydrate recognition domain]]

OCA at 08:57, 27 March 2013

2013-03-27T08:57:39Z

← Older revision		Revision as of 08:57, 27 March 2013
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	~~'''Unreleased~~ structure~~'''~~		{{STRUCTURE_4e52\| PDB=4e52 \| SCENE= }}
			===Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D===
			{{ABSTRACT_PUBMED_19799916}}

	~~The entry 4e52 is ON HOLD until Paper Publication~~		==Function==
			[[http://www.uniprot.org/uniprot/SFTPD_HUMAN SFTPD_HUMAN]] Contributes to the lung's defense against inhaled microorganisms. May participate in the extracellular reorganization or turnover of pulmonary surfactant. Binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.

	~~Authors~~: ~~Shrive, A~~.K.~~, Greenhough, T~~.J.		==About this Structure==
			[[4e52]] is a 3 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=4E52 OCA].

	~~Description~~: ~~Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant~~ protein D		==Reference==
			<ref group="xtra">PMID:019799916</ref><ref group="xtra">PMID:012888356</ref><references group="xtra"/><references/>
			[[Category: Homo sapiens]]
			[[Category: Greenhough, T J.]]
			[[Category: Shrive, A K.]]
			[[Category: Alpha-helical coiled coil]]
			[[Category: Carbohydrate recognition domain]]
			[[Category: Lectin]]
			[[Category: Neck+crd]]
			[[Category: Sugar binding protein]]
			[[Category: Trimeric recombinant collectin fragment]]

OCA at 07:11, 4 July 2012

2012-07-04T07:11:18Z

← Older revision		Revision as of 07:11, 4 July 2012
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4e52 is ON HOLD		The entry 4e52 is ON HOLD until Paper Publication

	Authors: Shrive, A.K., Greenhough, T.J.		Authors: Shrive, A.K., Greenhough, T.J.

	Description: Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D		Description: Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D

OCA at 08:44, 9 May 2012

2012-05-09T08:44:52Z

← Older revision		Revision as of 08:44, 9 May 2012
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4e52 is ON HOLD ~~until sometime in the future~~		The entry 4e52 is ON HOLD

	Authors: Shrive, A.K., Greenhough, T.J.		Authors: Shrive, A.K., Greenhough, T.J.

	Description: Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D		Description: Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D

OCA at 07:28, 18 April 2012

2012-04-18T07:28:53Z

← Older revision		Revision as of 07:28, 18 April 2012
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	'''Unreleased structure'''		'''Unreleased structure'''

	The entry 4e52 is ON HOLD		The entry 4e52 is ON HOLD until sometime in the future

	Authors: Shrive, A.K., Greenhough, T.J.		Authors: Shrive, A.K., Greenhough, T.J.

	Description: Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D		Description: Crystal structure of Haemophilus Eagan 4A polysaccharide bound human lung surfactant protein D