1NWV

SOLUTION STRUCTURE OF A FUNCTIONALLY ACTIVE COMPONENT OF DECAY ACCELERATING FACTOR

Summary for 1NWV

• Entry DOI: 10.2210/pdb1nwv/pdb
• NMR Information: BMRB: 5506
• Descriptor: Complement decay-accelerating factor (1 entity in total)
• Functional Keywords: cd55, daf, ccp, complement, biosynthetic protein
• Biological source: Homo sapiens (human)
• Cellular location: Isoform 1: Cell membrane; Single-pass type I membrane protein. Isoform 2: Cell membrane; Lipid-anchor, GPI- anchor: P08174
• Total number of polymer chains: 1
• Total formula weight: 14351.30

Authors

Uhrinova, S.,Lin, F.,Ball, G.,Bromek, K.,Uhrin, D.,Medof, M.E.,Barlow, P.N. (deposition date: 2003-02-07, release date: 2003-04-22, Last modification date: 2024-10-16)

Primary citation

Uhrinova, S.,Lin, F.,Ball, G.,Bromek, K.,Uhrin, D.,Medof, M.E.,Barlow, P.N.
Solution structure of a functionally active fragment of decay-accelerating factor
Proc.Natl.Acad.Sci.USA, 100:4718-4723, 2003

PubMed Abstract: The second and third modules of human decay accelerating factor (DAF) are necessary and sufficient to accelerate decay of the classical pathway (CP) convertase of complement. No structure of a mammalian protein with decay-accelerating activity has been available to date. We therefore determined the solution structure of DAF modules 2 and 3 (DAF approximately 2,3). Structure-guided analysis of 24 mutants identified likely contact points between DAF and the CP convertase. Three (R96, R69, and a residue in the vicinity of L171) lie on DAF approximately 2,3's concave face. A fourth, consisting of K127 and nearby R100, is on the opposite face. Regions of module 3 remote from the semiflexible 2-3 interface seem not to be involved in binding to the CP convertase. DAF thus seems to occupy a groove on the CP convertase such that both faces of DAF close to the 2-3 junction (including a positively charged region that encircles the protein at this point) interact simultaneously. Alternative pathway convertase interactions with DAF require additional regions of CCP 3 lying away from the 2-3 interface, consistent with the established additional requirement of module 4 for alternative pathway regulation.

PubMed: 12672958
DOI: 10.1073/pnas.0730844100

Experimental method

SOLUTION NMR