1buu
From Proteopedia
(New page: 200px<br /><applet load="1buu" size="450" color="white" frame="true" align="right" spinBox="true" caption="1buu, resolution 1.90Å" /> '''ONE HO3+ FORM OF RAT...) |
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| - | [[Image:1buu.gif|left|200px]]<br /><applet load="1buu" size=" | + | [[Image:1buu.gif|left|200px]]<br /><applet load="1buu" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1buu, resolution 1.90Å" /> | caption="1buu, resolution 1.90Å" /> | ||
'''ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A'''<br /> | '''ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A'''<br /> | ||
==Overview== | ==Overview== | ||
| - | C-type animal lectins are a diverse family of proteins which mediate | + | C-type animal lectins are a diverse family of proteins which mediate cell-surface carbohydrate-recognition events through a conserved carbohydrate-recognition domain (CRD). Most members of this family possess a carbohydrate-binding activity that depends strictly on the binding of Ca2+ at two sites, designated 1 and 2, in the CRD. The structural transitions associated with Ca2+ binding in C-type lectins have been investigated by determining high-resolution crystal structures of rat serum mannose-binding protein (MBP) bound to one Ho3+ in place of Ca2+, and the apo form of rat liver MBP. The removal of Ca2+ does not affect the core structure of the CRD, but dramatic conformational changes occur in the loops. The most significant structural change in the absence of Ca2+ is the isomerization of a cis-peptide bond preceding a conserved proline residue in Ca2+ site 2. This bond adopts the cis conformation in all Ca2+-bound structures, whereas both cis and trans conformations are observed in the absence of Ca2+. The pattern of structural changes in the three loops that interact with Ca2+ is dictated in large part by the conformation of the prolyl peptide bond. The highly conserved nature of Ca2+ site 2 suggests that the transitions observed in MBPs are general features of Ca2+ binding in C-type lectins. |
==About this Structure== | ==About this Structure== | ||
| - | 1BUU 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 HO as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1BUU 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 <scene name='pdbligand=HO:'>HO</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUU OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Ng, K | + | [[Category: Ng, K K.S.]] |
[[Category: Park-Snyder, S.]] | [[Category: Park-Snyder, S.]] | ||
| - | [[Category: Weis, W | + | [[Category: Weis, W I.]] |
[[Category: HO]] | [[Category: HO]] | ||
[[Category: host defense]] | [[Category: host defense]] | ||
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[[Category: metalloprotein]] | [[Category: metalloprotein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 11:59:20 2008'' |
Revision as of 09:59, 21 February 2008
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ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A
Overview
C-type animal lectins are a diverse family of proteins which mediate cell-surface carbohydrate-recognition events through a conserved carbohydrate-recognition domain (CRD). Most members of this family possess a carbohydrate-binding activity that depends strictly on the binding of Ca2+ at two sites, designated 1 and 2, in the CRD. The structural transitions associated with Ca2+ binding in C-type lectins have been investigated by determining high-resolution crystal structures of rat serum mannose-binding protein (MBP) bound to one Ho3+ in place of Ca2+, and the apo form of rat liver MBP. The removal of Ca2+ does not affect the core structure of the CRD, but dramatic conformational changes occur in the loops. The most significant structural change in the absence of Ca2+ is the isomerization of a cis-peptide bond preceding a conserved proline residue in Ca2+ site 2. This bond adopts the cis conformation in all Ca2+-bound structures, whereas both cis and trans conformations are observed in the absence of Ca2+. The pattern of structural changes in the three loops that interact with Ca2+ is dictated in large part by the conformation of the prolyl peptide bond. The highly conserved nature of Ca2+ site 2 suggests that the transitions observed in MBPs are general features of Ca2+ binding in C-type lectins.
About this Structure
1BUU is a Single protein structure of sequence from Rattus norvegicus with as ligand. Full crystallographic information is available from OCA.
Reference
Ca2+-dependent structural changes in C-type mannose-binding proteins., Ng KK, Park-Snyder S, Weis WI, Biochemistry. 1998 Dec 22;37(51):17965-76. PMID:9922165
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