Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
Pt 11
pubmed:dateCreated
2004-10-25
pubmed:abstractText
Aall-A and Aall-B, two novel heterodimeric snake-venom C-type lectin-like proteins (sv-CLPs), were purified from the venom of Deinagkistrodon acutus from Anhui, China. Strikingly, both these proteins can localize on and congregate human erythrocytes, instead of aiming at the common targets of sv-CLPs such as platelet glycoproteins, von Willebrand factors, coagulant factors etc. The crystals of Aall-A belong to space group P2, with unit-cell parameters a = 105.2, b = 56.2, c = 108.7 A, beta = 100.5 degrees , and diffract to 2.0 A resolution, while the crystals of Aall-B belong to space group P2(1)2(1)2(1), with unit-cell parameters a = 36.8, b = 56.5, c = 149.2 A, and diffract to 2.2 A resolution. To our knowledge, this is the first report of sv-CLPs with this unique function and of their preliminary crystallographic analysis.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0907-4449
pubmed:author
pubmed:issnType
Print
pubmed:volume
60
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2035-7
pubmed:dateRevised
2007-7-24
pubmed:meshHeading
pubmed:year
2004
pubmed:articleTitle
Purification, characterization, crystallization and preliminary X-ray crystallographic analysis of two novel C-type lectin-like proteins: Aall-A and Aall-B from Deinagkistrodon acutus venom.
pubmed:affiliation
Key Laboratory of Structural Biology, Chinese Academy of Sciences, University of Science and Technology of China, 96 Jinzhai Road, Hefei, Anhui 230026, People's Republic of China.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't