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1bch
From Proteopedia
(New page: 200px<br /> <applet load="1bch" size="450" color="white" frame="true" align="right" spinBox="true" caption="1bch, resolution 2.0Å" /> '''MANNOSE-BINDING PROT...) |
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==About this Structure== | ==About this Structure== | ||
| - | 1BCH 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 A2G, NGA, CA, CL and NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BCH OCA]]. | + | 1BCH 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 A2G, NGA, CA, CL and NA as [[http://en.wikipedia.org/wiki/ligands ligands]]. Structure known Active Sites: 11, 12, 13, 21, 22, 23, 31, 32 and 33. Full crystallographic information is available from [[http://ispc.weizmann.ac.il/oca-bin/ocashort?id=1BCH OCA]]. |
==Reference== | ==Reference== | ||
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[[Category: lectin]] | [[Category: lectin]] | ||
| - | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://ispc.weizmann.ac.il/oca OCA ] on Tue Oct 30 12:20:09 2007'' |
Revision as of 10:15, 30 October 2007
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MANNOSE-BINDING PROTEIN-A MUTANT (QPDWGH) COMPLEXED WITH N-ACETYL-D-GALACTOSAMINE
Overview
The mammalian hepatic asialoglycoprotein receptor, a member of the C-type, animal lectin family, displays preferential binding to, N-acetylgalactosamine compared with galactose. The structural basis for, selective binding to N-acetylgalactosamine has been investigated. Regions, of the carbohydrate-recognition domain of the receptor believed to be, important in preferential binding to N-acetylgalactosamine have been, inserted into the homologous carbohydrate-recognition domain of a, mannose-binding protein mutant that was previously altered to bind, galactose. Introduction of a single histidine residue corresponding to, residue 256 of the hepatic asialoglycoprotein receptor was found to cause, a 14-fold increase in the relative affinity for N-acetylgalactosamine, compared with galactose. ... [(full description)]
About this Structure
1BCH is a [Single protein] structure of sequence from [Rattus norvegicus] with A2G, NGA, CA, CL and NA as [ligands]. Structure known Active Sites: 11, 12, 13, 21, 22, 23, 31, 32 and 33. Full crystallographic information is available from [OCA].
Reference
Mechanism of N-acetylgalactosamine binding to a C-type animal lectin carbohydrate-recognition domain., Kolatkar AR, Leung AK, Isecke R, Brossmer R, Drickamer K, Weis WI, J Biol Chem. 1998 Jul 31;273(31):19502-8. PMID:9677372
Page seeded by OCA on Tue Oct 30 12:20:09 2007
Categories: Rattus norvegicus | Single protein | Kolatkar, A.R. | Weis, W.I. | A2G | CA | CL | NA | NGA | C-type lectin | Calcium-binding protein | Lectin
