3a5p: Difference between revisions
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==Crystal structure of hemagglutinin== | |||
=== | <StructureSection load='3a5p' size='340' side='right' caption='[[3a5p]], [[Resolution|resolution]] 1.82Å' scene=''> | ||
== Structural highlights == | |||
<table><tr><td colspan='2'>[[3a5p]] is a 4 chain structure with sequence from [http://en.wikipedia.org/wiki/Phypo Phypo]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=3A5P OCA]. For a <b>guided tour on the structure components</b> use [http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=3A5P FirstGlance]. <br> | |||
</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=3a5p FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=3a5p OCA], [http://www.rcsb.org/pdb/explore.do?structureId=3a5p RCSB], [http://www.ebi.ac.uk/pdbsum/3a5p PDBsum]</span></td></tr> | |||
</table> | |||
<div style="background-color:#fffaf0;"> | |||
== Publication Abstract from PubMed == | |||
Physarum polycephalum hemagglutinin I (HA1) is a 104-residue protein that is secreted to extracellular space. The crystal structure of HA1 has a beta-sandwich fold found among lectin structures, such as legume lectins and galectins. Interestingly, the beta-sandwich of HA1 lacks a jelly roll motif and is essentially composed of two simple up-and-down beta-sheets. This up-and-down beta-sheet motif is well conserved in other legume lectin-like proteins derived from animals, plants, bacteria, and viruses. It is more noteworthy that the up-and-down beta-sheet motif includes many residues that make contact with the target carbohydrates. Our NMR data demonstrate that HA1 lacking a jelly roll motif also binds to its target glycopeptide. Taken together, these data show that the up-and-down beta-sheet motif provides a fundamental scaffold for the binding of legume lectin-like proteins to the target carbohydrates, and the structure of HA1 suggests a minimal carbohydrate recognition domain. | |||
The Structure of Physarum polycephalum Hemagglutinin I Suggests a Minimal Carbohydrate Recognition Domain of Legume Lectin Fold.,Kouno T, Watanabe N, Sakai N, Nakamura T, Nabeshima Y, Morita M, Mizuguchi M, Aizawa T, Demura M, Imanaka T, Tanaka I, Kawano K J Mol Biol. 2010 Nov 20. PMID:21094650<ref>PMID:21094650</ref> | |||
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.<br> | |||
</div> | |||
==See Also== | ==See Also== | ||
*[[Hemagglutinin|Hemagglutinin]] | *[[Hemagglutinin|Hemagglutinin]] | ||
== References == | |||
== | <references/> | ||
__TOC__ | |||
</StructureSection> | |||
[[Category: Phypo]] | [[Category: Phypo]] | ||
[[Category: Kawano, K | [[Category: Kawano, K]] | ||
[[Category: Kouno, T | [[Category: Kouno, T]] | ||
[[Category: Mizuguchi, M | [[Category: Mizuguchi, M]] | ||
[[Category: Nabeshima, Y | [[Category: Nabeshima, Y]] | ||
[[Category: Nakamura, T | [[Category: Nakamura, T]] | ||
[[Category: Sakai, N | [[Category: Sakai, N]] | ||
[[Category: Watanabe, N | [[Category: Watanabe, N]] | ||
[[Category: Lectin]] | [[Category: Lectin]] | ||
[[Category: Sugar binding protein]] | [[Category: Sugar binding protein]] | ||
Revision as of 19:49, 21 December 2014
Crystal structure of hemagglutininCrystal structure of hemagglutinin
Structural highlights
Publication Abstract from PubMedPhysarum polycephalum hemagglutinin I (HA1) is a 104-residue protein that is secreted to extracellular space. The crystal structure of HA1 has a beta-sandwich fold found among lectin structures, such as legume lectins and galectins. Interestingly, the beta-sandwich of HA1 lacks a jelly roll motif and is essentially composed of two simple up-and-down beta-sheets. This up-and-down beta-sheet motif is well conserved in other legume lectin-like proteins derived from animals, plants, bacteria, and viruses. It is more noteworthy that the up-and-down beta-sheet motif includes many residues that make contact with the target carbohydrates. Our NMR data demonstrate that HA1 lacking a jelly roll motif also binds to its target glycopeptide. Taken together, these data show that the up-and-down beta-sheet motif provides a fundamental scaffold for the binding of legume lectin-like proteins to the target carbohydrates, and the structure of HA1 suggests a minimal carbohydrate recognition domain. The Structure of Physarum polycephalum Hemagglutinin I Suggests a Minimal Carbohydrate Recognition Domain of Legume Lectin Fold.,Kouno T, Watanabe N, Sakai N, Nakamura T, Nabeshima Y, Morita M, Mizuguchi M, Aizawa T, Demura M, Imanaka T, Tanaka I, Kawano K J Mol Biol. 2010 Nov 20. PMID:21094650[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. See AlsoReferences
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