RGD Reference Report - Asymmetry adjacent to the collagen-like domain in rat liver mannose-binding protein. - Rat Genome Database

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Asymmetry adjacent to the collagen-like domain in rat liver mannose-binding protein.

Authors: Wallis, R  Drickamer, K 
Citation: Wallis R and Drickamer K, Biochem J. 1997 Jul 15;325 ( Pt 2):391-400.
RGD ID: 1582157
Pubmed: PMID:9230118   (View Abstract at PubMed)
PMCID: PMC1218572   (View Article at PubMed Central)

Rat liver mannose-binding protein (MBP-C) is the smallest known member of the collectin family of animal lectins, many of which are involved in defence against microbial pathogens. It consists of an N-terminal collagen-like domain linked to C-terminal carbohydrate-recognition domains. MBP-C, overproduced in Chinese-hamster ovary cells, is post-translationally modified and processed in a manner similar to the native lectin. Analytical ultracentrifugation experiments indicate that MBP-C is trimeric, with a weight-averaged molecular mass of approx. 77 kDa. The rate of sedimentation of MBP-C and its mobility on gel filtration suggest a highly elongated molecule. Anomalous behaviour on gel filtration due to this extended conformation may explain previous suggestions that MBP-C forms a higher oligomer. The polypeptide chains of the MBP-C trimer are linked by disulphide bonds between two cysteine residues at the N-terminal junction of the collagen-like domain. Analysis of an N-terminal tryptic fragment reveals that the disulphide bonding in MBP-C is heterogeneous and asymmetrical. These results indicate that assembly of MBP-C oligomers probably proceeds in a C- to N-terminal direction: trimerization at the C-terminus is followed by assembly of the collagenous domain and finally formation of N-terminal disulphide bonds. The relatively simple organization of MBP-C provides a template for understanding larger, more complex collectins.

Gene Ontology Annotations    Click to see Annotation Detail View

Molecular Function
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
identical protein binding  IPIMbl2 (Rattus norvegicus)1582157homotrimerizationRGD 

Objects Annotated

Genes (Rattus norvegicus)
Mbl2  (mannose binding lectin 2)


Additional Information