PMID- 10368295
OWN - NLM
STAT- MEDLINE
DCOM- 19990506
LR  - 20170804
IS  - 0969-2126 (Print)
IS  - 0969-2126 (Linking)
VI  - 7
IP  - 3
DP  - 1999 Mar 15
TI  - Crystal structure of the trimeric alpha-helical coiled-coil and the three lectin 
      domains of human lung surfactant protein D.
PG  - 255-64
AB  - BACKGROUND: Human lung surfactant protein D (hSP-D) belongs to the collectin
      family of C-type lectins and participates in the innate immune surveillance
      against microorganisms in the lung through recognition of carbohydrate ligands
      present on the surface of pathogens. The involvement of this protein in innate
      immunity and the allergic response make it the subject of much interest. RESULTS:
      We have determined the crystal structure of a trimeric fragment of hSP-D at 2.3 A
      resolution. The structure comprises an alpha-helical coiled-coil and three
      carbohydrate-recognition domains (CRDs). An interesting deviation from symmetry
      was found in the projection of a single tyrosine sidechain into the centre of the
      coiled-coil; the asymmetry of this residue influences the orientation of one of
      the adjacent CRDs. The cleft between the three CRDs presents a large positively
      charged surface. CONCLUSIONS: The fold of the CRD of hSP-D is similar to that of 
      the mannan-binding protein (MBP), but its orientation relative to the
      alpha-helical coiled-coil region differs somewhat to that seen in the MBP
      structure. The novel central packing of the tyrosine sidechain within the
      coiled-coil and the resulting asymmetric orientation of the CRDs has unexpected
      functional implications. The positively charged surface might facilitate binding 
      to negatively charged structures, such as lipopolysaccharides.
FAU - Hakansson, K
AU  - Hakansson K
AD  - Department of Microbiology, University of Illinois at Urbana-Champaign, B103
      CLSL, 601 South Goodwin Avenue, Urbana, IL 61801, USA. kjell@scs.uiuc.edu
FAU - Lim, N K
AU  - Lim NK
FAU - Hoppe, H J
AU  - Hoppe HJ
FAU - Reid, K B
AU  - Reid KB
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Structure
JT  - Structure (London, England : 1993)
JID - 101087697
RN  - 0 (Glycoproteins)
RN  - 0 (Lectins)
RN  - 0 (Pulmonary Surfactant-Associated Protein D)
RN  - 0 (Pulmonary Surfactants)
RN  - 0 (Recombinant Fusion Proteins)
RN  - SY7Q814VUP (Calcium)
SB  - IM
MH  - Amino Acid Sequence
MH  - Binding Sites
MH  - Calcium/chemistry
MH  - Crystallography, X-Ray
MH  - Glycoproteins/*chemistry
MH  - Humans
MH  - Lectins
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - *Protein Conformation
MH  - Protein Structure, Secondary
MH  - Pulmonary Surfactant-Associated Protein D
MH  - Pulmonary Surfactants/*chemistry
MH  - Recombinant Fusion Proteins/chemistry
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
EDAT- 1999/06/16 00:00
MHDA- 1999/06/16 00:01
CRDT- 1999/06/16 00:00
PHST- 1999/06/16 00:00 [pubmed]
PHST- 1999/06/16 00:01 [medline]
PHST- 1999/06/16 00:00 [entrez]
AID - S0969-2126(99)80036-7 [pii]
PST - ppublish
SO  - Structure. 1999 Mar 15;7(3):255-64.