Linked Life Data

19501100

Source:http://linkedlifedata.com/resource/pubmed/id/19501100

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1
pubmed:dateCreated
2009-7-20
pubmed:abstractText
Mannan-binding lectin (MBL) is the archetypical pathogen recognition molecule of the innate immune defense. Upon binding to microorganisms, reactions leading to the destruction of the offender ensue. MBL is an oligomer of structural subunits each composed of three identical polypeptides. We used atomic force microscopy to reveal tertiary and quaternary structures of MBL. The images in both air and buffer show a quaternary structure best described as "sertiform", that is, a hub from which the subunits fan out. The dimensions conform to those calculated from primary and secondary structures. The subunits associate with a preferred angle of 40 degrees between them. This angle is stable with respect to the degree of oligomerization for MBL of four subunits or more. Due to an interruption in the collagenous sequence, the arms of the subunits are expected to form a kink. We find that approximately 30% of the subunits are kinked and the kink angle distributed, quite broadly, around 145 degrees . The conformation and flexibility of the MBL molecule that we observe differ distinctly from the popular view of a "bouquet-like" configuration as that found for related members of the complement system such as C1q. This structural information will further the understanding of the specific functioning of the MBL pathway of complement activation.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
1089-8638
pubmed:author
pubmed:issnType
Electronic
pubmed:day
7
pubmed:volume
391
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
246-59
pubmed:meshHeading
pubmed:year
2009
pubmed:articleTitle
Mannan-binding lectin: structure, oligomerization, and flexibility studied by atomic force microscopy.
pubmed:affiliation
Leiden Institute of Physics, Leiden University, Niels Bohrweg 2, Leiden, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't