1hup
From Proteopedia
(New page: 200px<br /> <applet load="1hup" size="450" color="white" frame="true" align="right" spinBox="true" caption="1hup, resolution 2.5Å" /> '''HUMAN MANNOSE BINDIN...) |
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| - | [[Image:1hup.gif|left|200px]]<br /> | + | [[Image:1hup.gif|left|200px]]<br /><applet load="1hup" size="350" color="white" frame="true" align="right" spinBox="true" |
| - | <applet load="1hup" size=" | + | |
caption="1hup, resolution 2.5Å" /> | caption="1hup, resolution 2.5Å" /> | ||
'''HUMAN MANNOSE BINDING PROTEIN CARBOHYDRATE RECOGNITION DOMAIN TRIMERIZES THROUGH A TRIPLE ALPHA-HELICAL COILED-COIL'''<br /> | '''HUMAN MANNOSE BINDING PROTEIN CARBOHYDRATE RECOGNITION DOMAIN TRIMERIZES THROUGH A TRIPLE ALPHA-HELICAL COILED-COIL'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Human mannose-binding protein is a hexamer of trimers with each subunit | + | Human mannose-binding protein is a hexamer of trimers with each subunit consisting of an amino-terminal region rich in cysteine, 19 collagen repeats, a 'neck', and a carbohydrate recognition domain that requires calcium to bind ligand. A 148-residue peptide, consisting of the 'neck' and carbohydrate recognition domains forms trimers in solution and in crystals. The structure of this trimeric peptide has been determined in two different crystal forms. The 'neck' forms a triple alpha-helical coiled-coil. Each alpha-helix interacts with a neighbouring carbohydrate recognition domain. The spatial arrangement of the carbohydrate recognition domains suggest how MBP trimers form the basic recognition unit for branched oligosaccharides on microorganisms. |
==About this Structure== | ==About this Structure== | ||
| - | 1HUP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with CA and SO4 as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http:// | + | 1HUP is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Homo_sapiens Homo sapiens] with <scene name='pdbligand=CA:'>CA</scene> and <scene name='pdbligand=SO4:'>SO4</scene> as [http://en.wikipedia.org/wiki/ligands ligands]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1HUP OCA]. |
==Reference== | ==Reference== | ||
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[[Category: alpha-helical coiled-coil]] | [[Category: alpha-helical coiled-coil]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 13:05:03 2008'' |
Revision as of 11:05, 21 February 2008
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HUMAN MANNOSE BINDING PROTEIN CARBOHYDRATE RECOGNITION DOMAIN TRIMERIZES THROUGH A TRIPLE ALPHA-HELICAL COILED-COIL
Overview
Human mannose-binding protein is a hexamer of trimers with each subunit consisting of an amino-terminal region rich in cysteine, 19 collagen repeats, a 'neck', and a carbohydrate recognition domain that requires calcium to bind ligand. A 148-residue peptide, consisting of the 'neck' and carbohydrate recognition domains forms trimers in solution and in crystals. The structure of this trimeric peptide has been determined in two different crystal forms. The 'neck' forms a triple alpha-helical coiled-coil. Each alpha-helix interacts with a neighbouring carbohydrate recognition domain. The spatial arrangement of the carbohydrate recognition domains suggest how MBP trimers form the basic recognition unit for branched oligosaccharides on microorganisms.
About this Structure
1HUP is a Single protein structure of sequence from Homo sapiens with and as ligands. Full crystallographic information is available from OCA.
Reference
Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil., Sheriff S, Chang CY, Ezekowitz RA, Nat Struct Biol. 1994 Nov;1(11):789-94. PMID:7634089
Page seeded by OCA on Thu Feb 21 13:05:03 2008
