2kmb: Difference between revisions
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[[Image:2kmb.gif|left|200px]]<br /> | [[Image:2kmb.gif|left|200px]]<br /><applet load="2kmb" size="450" color="white" frame="true" align="right" spinBox="true" | ||
<applet load="2kmb" size="450" color="white" frame="true" align="right" spinBox="true" | |||
caption="2kmb, resolution 2.0Å" /> | caption="2kmb, resolution 2.0Å" /> | ||
'''COMPLEX OF 3'-NEUAC-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A'''<br /> | '''COMPLEX OF 3'-NEUAC-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A'''<br /> | ||
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==About this Structure== | ==About this Structure== | ||
2KMB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. | 2KMB is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus] with CA and CL as [http://en.wikipedia.org/wiki/ligands ligands]. Known structural/functional Sites: <scene name='pdbsite=11:Ca Site 1, Protomer 1'>11</scene>, <scene name='pdbsite=12:Ca Site 1, Protomer 2'>12</scene>, <scene name='pdbsite=13:Ca Site 1, Protomer 3'>13</scene>, <scene name='pdbsite=21:Ca Site 2, Protomer 1'>21</scene>, <scene name='pdbsite=22:Ca Site 2, Protomer 2'>22</scene>, <scene name='pdbsite=23:Ca Site 2, Protomer 3'>23</scene>, <scene name='pdbsite=31:Ca Site 3, Protomer 1'>31</scene>, <scene name='pdbsite=32:Ca Site 3, Protomer 2'>32</scene> and <scene name='pdbsite=33:Ca Site 3, Protomer 3'>33</scene>. Full crystallographic information is available from [http://ispc.weizmann.ac.il/oca-bin/ocashort?id=2KMB OCA]. | ||
==Reference== | ==Reference== | ||
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[[Category: lectin]] | [[Category: lectin]] | ||
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Revision as of 21:02, 18 December 2007
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COMPLEX OF 3'-NEUAC-LEWIS-X WITH A SELECTIN-LIKE MUTANT OF MANNOSE-BINDING PROTEIN A
OverviewOverview
Rat serum mannose-binding protein in which residues 211-213 have been, changed to the Lys-Lys-Lys sequence found in E-selectin binds HL-60 cells, and the oligosaccharide 3'-NeuAc-Le(x). To understand how this mutant, designated K3, mimics the carbohydrate-binding properties of E-selectin, structures of K3 alone and in complexes with 3'-NeuAc-Le(x), 3'-sulfo-Le(x) and 4'-sulfo-Le(x) have been determined at 1.95-2.1 A, resolution by X-ray crystallography. The region of K3 that interacts with, bound oligosaccharides superimposes closely with the corresponding region, of unliganded E-selectin. In each of the oligosaccharide-protein, complexes, the 2- and 3-OH of Fuc coordinate Ca2+ and form a network of, cooperative hydrogen bonds with amino acid side chains that also, coordinate the Ca2+. Lys211 of the K3 mutant, which corresponds to Lys111, of E-selectin, interacts with each of the three bound ligands: the N zeta, atom donates a hydrogen bond to the 4-OH of Gal in 3'-NeuAc-Le(x), forms a, water-mediated hydrogen bond with the 4-OH of Gal in 3'-sulfo-Le(x), and, forms a salt bridge with the sulfate group of 4'-sulfo-Le(x). Lys213 packs, against an otherwise exposed aromatic residue and forms a water-mediated, hydrogen bond with Lys211 which may help to position that residue for, interactions with bound oligosaccharides. These structures are consistent, with previous mutagenesis and chemical modification studies which, demonstrate the importance of the Ca2+ ligands as well as Lys111 and, Lys113 for carbohydrate binding in the selectins, and they provide a, structural basis for understanding the selective recognition of negatively, charged Le(x) derivatives by the selectins.
About this StructureAbout this Structure
2KMB is a Single protein structure of sequence from Rattus norvegicus with CA and CL as ligands. Known structural/functional Sites: , , , , , , , and . Full crystallographic information is available from OCA.
ReferenceReference
Structure of a selectin-like mutant of mannose-binding protein complexed with sialylated and sulfated Lewis(x) oligosaccharides., Ng KK, Weis WI, Biochemistry. 1997 Feb 4;36(5):979-88. PMID:9033386
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