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| - | [[Image:1rtm.gif|left|200px]] | + | {{Seed}} |
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| | {{STRUCTURE_1rtm| PDB=1rtm | SCENE= }} | | {{STRUCTURE_1rtm| PDB=1rtm | SCENE= }} |
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| - | '''TRIMERIC STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN'''
| + | ===TRIMERIC STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN=== |
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| - | ==Overview==
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| - | BACKGROUND: Mannose-binding proteins (MBPs) are C-type (Ca(2+)-dependent) animal lectins found in serum. They recognize cell-surface oligosaccharide structures characteristic of pathogenic bacteria and fungi, and trigger the neutralization of these organisms. Like most lectins, MBPs display weak intrinsic affinity for monovalent sugar ligands, but bind avidly to multivalent ligands. RESULTS: We report physical studies in solution and the crystal structure determined at 1.8 A Bragg spacings of a trimeric fragment of MBP-A, containing the carbohydrate-recognition domain (CRD) and the neck domain that links the carboxy-terminal CRD to the collagen-like portion of the intact molecule. The neck consists of a parallel triple-stranded coiled coil of alpha-helices linked by four residues to the CRD. The isolated neck peptide does not form stable helices in aqueous solution. The previously characterized carbohydrate-binding sites lie at the distal end of the trimer and are separated from each other by 53 A. CONCLUSIONS: The carbohydrate-binding sites in MBP-A are too far apart for a single trimer to bind multivalently to a typical mammalian high-mannose oligosaccharide. Thus MBPs can recognize pathogens selectively by binding avidly only to the widely spaced, repetitive sugar arrays on pathogenic cell surfaces. Sequence alignments reveal that other C-type lectins are likely to have a similar oligomeric structure, but differences in their detailed organization will have an important role in determining their interactions with oligosaccharides.
| + | The line below this paragraph, {{ABSTRACT_PUBMED_7704532}}, adds the Publication Abstract to the page |
| | + | (as it appears on PubMed at http://www.pubmed.gov), where 7704532 is the PubMed ID number. |
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| | + | {{ABSTRACT_PUBMED_7704532}} |
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| | ==About this Structure== | | ==About this Structure== |
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| | [[Category: Weis, W I.]] | | [[Category: Weis, W I.]] |
| | [[Category: Lectin]] | | [[Category: Lectin]] |
| - | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sat May 3 07:53:34 2008'' | + | |
| | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Sun Jul 27 15:07:32 2008'' |
Revision as of 12:07, 27 July 2008
Template:STRUCTURE 1rtm
TRIMERIC STRUCTURE OF A C-TYPE MANNOSE-BINDING PROTEIN
Template:ABSTRACT PUBMED 7704532
About this Structure
1RTM is a Single protein structure of sequence from Rattus norvegicus. Full crystallographic information is available from OCA.
Reference
Trimeric structure of a C-type mannose-binding protein., Weis WI, Drickamer K, Structure. 1994 Dec 15;2(12):1227-40. PMID:7704532
Page seeded by OCA on Sun Jul 27 15:07:32 2008
