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| - | [[Image:1bv4.gif|left|200px]] | + | {{Seed}} |
| | + | [[Image:1bv4.png|left|200px]] |
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| | {{STRUCTURE_1bv4| PDB=1bv4 | SCENE= }} | | {{STRUCTURE_1bv4| PDB=1bv4 | SCENE= }} |
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| - | '''APO-MANNOSE-BINDING PROTEIN-C'''
| + | ===APO-MANNOSE-BINDING PROTEIN-C=== |
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| - | ==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 |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 9922165 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_9922165}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Calcium-binding protein]] | | [[Category: Calcium-binding protein]] |
| | [[Category: Collectin]] | | [[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 Mon Jun 30 19:46:02 2008'' |
Revision as of 16:46, 30 June 2008
Template:STRUCTURE 1bv4
APO-MANNOSE-BINDING PROTEIN-C
Template:ABSTRACT PUBMED 9922165
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 Mon Jun 30 19:46:02 2008
