1r14

<table><tr><td colspan='2'>[[1r14]] is a 1 chain structure with sequence from [http://en.wikipedia.org/wiki/Buffalo_rat Buffalo rat]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1R14 OCA]. For a <b>guided tour on the structure components</b> use [http://proteopedia.org/fgij/fg.htm?mol=1R14 FirstGlance]. <br>

</td></tr><tr id='ligand'><td class="sblockLbl"><b>[[Ligand|Ligands:]]</b></td><td class="sblockDat" id="ligandDat"><scene name='pdbligand=MES:2-(N-MORPHOLINO)-ETHANESULFONIC+ACID'>MES</scene>, <scene name='pdbligand=SM:SAMARIUM+(III)+ION'>SM</scene></td></tr>

<tr id='related'><td class="sblockLbl"><b>[[Related_structure|Related:]]</b></td><td class="sblockDat"><div style='overflow: auto; max-height: 3em;'>[[1r13|1r13]]</div></td></tr>

<tr id='gene'><td class="sblockLbl"><b>[[Gene|Gene:]]</b></td><td class="sblockDat">SFTPA1 OR SFTPA OR SFTP1 OR SFTP-1 ([http://www.ncbi.nlm.nih.gov/Taxonomy/Browser/wwwtax.cgi?mode=Info&srchmode=5&id=10116 Buffalo rat])</td></tr>

<tr id='resources'><td class="sblockLbl"><b>Resources:</b></td><td class="sblockDat"><span class='plainlinks'>[http://proteopedia.org/fgij/fg.htm?mol=1r14 FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1r14 OCA], [http://pdbe.org/1r14 PDBe], [http://www.rcsb.org/pdb/explore.do?structureId=1r14 RCSB], [http://www.ebi.ac.uk/pdbsum/1r14 PDBsum], [http://prosat.h-its.org/prosat/prosatexe?pdbcode=1r14 ProSAT]</span></td></tr>

[[http://www.uniprot.org/uniprot/SFTPA_RAT SFTPA_RAT]] In presence of calcium ions, it binds to surfactant phospholipids and contributes to lower the surface tension at the air-liquid interface in the alveoli of the mammalian lung and is essential for normal respiration.

<div style="background-color:#fffaf0;">

== Publication Abstract from PubMed ==

Surfactant protein A (SP-A), one of four proteins associated with pulmonary surfactant, binds with high affinity to alveolar phospholipid membranes, positioning the protein at the first line of defense against inhaled pathogens. SP-A exhibits both calcium-dependent carbohydrate binding, a characteristic of the collectin family, and specific interactions with lipid membrane components. The crystal structure of the trimeric carbohydrate recognition domain and neck domain of SP-A was solved to 2.1-A resolution with multiwavelength anomalous dispersion phasing from samarium. Two metal binding sites were identified, one in the highly conserved lectin site and the other 8.5 A away. The interdomain carbohydrate recognition domain-neck angle is significantly less in SP-A than in the homologous collectins, surfactant protein D, and mannose-binding protein. This conformational difference may endow the SP-A trimer with a more extensive hydrophobic surface capable of binding lipophilic membrane components. The appearance of this surface suggests a putative binding region for membrane-derived SP-A ligands such as phosphatidylcholine and lipid A, the endotoxic lipid component of bacterial lipopolysaccharide that mediates the potentially lethal effects of Gram-negative bacterial infection.

Crystal structure of trimeric carbohydrate recognition and neck domains of surfactant protein A.,Head JF, Mealy TR, McCormack FX, Seaton BA J Biol Chem. 2003 Oct 31;278(44):43254-60. Epub 2003 Aug 11. PMID:12913002<ref>PMID:12913002</ref>

From MEDLINE&reg;/PubMed&reg;, a database of the U.S. National Library of Medicine.<br>

</div>

<div class="pdbe-citations 1r14" style="background-color:#fffaf0;"></div>

== References ==

<references/>

[[Category: Buffalo rat]]

[[Category: Head, J F]]

[[Category: McCormack, F X]]

[[Category: Mealy, T R]]

[[Category: Seaton, B A]]

[[Category: Alpha helical neck region]]

[[Category: Sugar binding protein]]