1buu: Difference between revisions

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[[Image:1buu.gif|left|200px]]
{{Seed}}
[[Image:1buu.png|left|200px]]


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{{STRUCTURE_1buu|  PDB=1buu  |  SCENE=  }}  
{{STRUCTURE_1buu|  PDB=1buu  |  SCENE=  }}  


'''ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A'''
===ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A===




==Overview==
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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.
The line below this paragraph, {{ABSTRACT_PUBMED_9922165}}, adds the Publication Abstract to the page
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{{ABSTRACT_PUBMED_9922165}}


==About this Structure==
==About this Structure==
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[[Category: Lectin]]
[[Category: Lectin]]
[[Category: Metalloprotein]]
[[Category: Metalloprotein]]
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Fri May  2 11:58:53 2008''
 
''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Mon Jun 30 19:45:21 2008''

Revision as of 16:45, 30 June 2008

File:1buu.png

Template:STRUCTURE 1buu

ONE HO3+ FORM OF RAT MANNOSE-BINDING PROTEIN A

Template:ABSTRACT PUBMED 9922165

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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