1buu

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[[Image:1buu.gif|left|200px]]
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{{Structure
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|RESOURCES=<span class='plainlinks'>[http://oca.weizmann.ac.il/oca-docs/fgij/fg.htm?mol=1buu FirstGlance], [http://oca.weizmann.ac.il/oca-bin/ocaids?id=1buu OCA], [http://www.ebi.ac.uk/pdbsum/1buu PDBsum], [http://www.rcsb.org/pdb/explore.do?structureId=1buu RCSB]</span>
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'''ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A'''
'''ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A'''
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[[Category: Park-Snyder, S.]]
[[Category: Park-Snyder, S.]]
[[Category: Weis, W I.]]
[[Category: Weis, W I.]]
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[[Category: host defense]]
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[[Category: Host defense]]
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[[Category: lectin]]
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[[Category: Lectin]]
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[[Category: metalloprotein]]
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[[Category: Metalloprotein]]
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:58:53 2008''
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''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:08:52 2008''
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Revision as of 08:58, 2 May 2008

Template:STRUCTURE 1buu

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. 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 Page seeded by OCA on Fri May 2 11:58:53 2008

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