Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1993-10-20
pubmed:abstractText
Barley lectin (BL) and its precursor form (proBL), synthesized and over-expressed in Escherichia coli, have been crystallized under conditions identical to those used for the closely related lectin wheat germ agglutinin. These lectins are members of the Gramineae family and possess a unique disulfide-rich domain structure. The pro-lectin polypeptides are extended by 15 amino acid residues at the carboxy terminus. This pro-peptide, which is proteolytically removed as the mature lectin is deposited in the vacuoles, is thought to function as a targeting signal for molecular sorting. Crystals of BL and proBL are well ordered and belong to space groups C222(1) and P2(1)2(1)2(1). The unit cell dimensions for BL and proBL are a = 51.9 A, b = 73.7 A, c = 89.3 A (one monomer per asymmetric unit), and a = 45.2 A, b = 70.5 A, c = 111.6 A (two monomers per asymmetric unit), respectively. Diffraction patterns on precession photographs of BL crystals are closely similar to those of mature wheat germ agglutinin crystals, suggesting similar crystal packing and correct conformation of this recombinant protein in terms of the four structural domains and 16 disulfide bridges.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0022-2836
pubmed:author
pubmed:issnType
Print
pubmed:day
20
pubmed:volume
233
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
322-4
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
1993
pubmed:articleTitle
Crystallization and preliminary X-ray diffraction studies of recombinant barley lectin and pro-barley lectin.
pubmed:affiliation
Department of Biochemistry and Molecular Biophysics, Virginia Commonwealth University, Richmond 23298.
pubmed:publicationType
Journal Article, Comparative Study, Research Support, U.S. Gov't, P.H.S.