1bv4
From Proteopedia
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[[Image:1bv4.gif|left|200px]] | [[Image:1bv4.gif|left|200px]] | ||
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'''APO-MANNOSE-BINDING PROTEIN-C''' | '''APO-MANNOSE-BINDING PROTEIN-C''' | ||
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[[Category: Ng, K K.S.]] | [[Category: Ng, K K.S.]] | ||
[[Category: Weis, W I.]] | [[Category: Weis, W I.]] | ||
- | [[Category: | + | [[Category: C-type lectin]] |
- | [[Category: | + | [[Category: Calcium-binding protein]] |
- | [[Category: | + | [[Category: Collectin]] |
- | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May 2 11:59:28 2008'' | |
- | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + |
Revision as of 08:59, 2 May 2008
APO-MANNOSE-BINDING PROTEIN-C
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
1BV4 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 11:59:28 2008