1buu: Difference between revisions
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[[Image:1buu.gif|left|200px]] | [[Image:1buu.gif|left|200px]] | ||
'''ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A''' | {{Structure | ||
|PDB= 1buu |SIZE=350|CAPTION= <scene name='initialview01'>1buu</scene>, resolution 1.90Å | |||
|SITE= | |||
|LIGAND= <scene name='pdbligand=HO:HOLMIUM ATOM'>HO</scene> | |||
|ACTIVITY= | |||
|GENE= | |||
}} | |||
'''ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A''' | |||
==Overview== | ==Overview== | ||
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==About this Structure== | ==About this Structure== | ||
1BUU is a [ | 1BUU is a [[Single protein]] structure of sequence from [http://en.wikipedia.org/wiki/Rattus_norvegicus Rattus norvegicus]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1BUU OCA]. | ||
==Reference== | ==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:[http:// | 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:[http://www.ncbi.nlm.nih.gov/pubmed/9922165 9922165] | ||
[[Category: Rattus norvegicus]] | [[Category: Rattus norvegicus]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
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[[Category: metalloprotein]] | [[Category: metalloprotein]] | ||
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Mar 20 10:16:04 2008'' | ||
Revision as of 08:16, 20 March 2008
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| 1buu, resolution 1.90Å | |||||||||||||
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| Ligands: | HO | ||||||||||||
| 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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