1buu
From Proteopedia
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|PDB= 1buu |SIZE=350|CAPTION= <scene name='initialview01'>1buu</scene>, resolution 1.90Å | |PDB= 1buu |SIZE=350|CAPTION= <scene name='initialview01'>1buu</scene>, resolution 1.90Å | ||
|SITE= | |SITE= | ||
| - | |LIGAND= <scene name='pdbligand=HO:HOLMIUM ATOM'>HO</scene> | + | |LIGAND= <scene name='pdbligand=HO:HOLMIUM+ATOM'>HO</scene> |
|ACTIVITY= | |ACTIVITY= | ||
|GENE= | |GENE= | ||
| + | |DOMAIN= | ||
| + | |RELATEDENTRY= | ||
| + | |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> | ||
}} | }} | ||
| Line 25: | Line 28: | ||
[[Category: Park-Snyder, S.]] | [[Category: Park-Snyder, S.]] | ||
[[Category: Weis, W I.]] | [[Category: Weis, W I.]] | ||
| - | [[Category: HO]] | ||
[[Category: host defense]] | [[Category: host defense]] | ||
[[Category: lectin]] | [[Category: lectin]] | ||
[[Category: metalloprotein]] | [[Category: metalloprotein]] | ||
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Mar 30 19:08:52 2008'' |
Revision as of 16:08, 30 March 2008
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| , resolution 1.90Å | |||||||
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| Ligands: | |||||||
| Resources: | FirstGlance, OCA, PDBsum, RCSB | ||||||
| Coordinates: | save as pdb, mmCIF, xml | ||||||
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
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