PMID- 17979752
OWN - NLM
STAT- MEDLINE
DCOM- 20080321
LR  - 20190728
IS  - 1873-4286 (Electronic)
IS  - 1381-6128 (Linking)
VI  - 13
IP  - 30
DP  - 2007
TI  - Human defensins: synthesis and structural properties.
PG  - 3096-118
AB  - Defensins are small, beta-sheet-rich, cationic peptides found in many organisms. 
      All defensins have amphiphilic properties, which are central for antimicrobial 
      activities of the proteins. The human genome encodes many defensin-line 
      molecules, of which 10 have been characterized. Molecules of all known human 
      defensins are stabilized by three intramolecular disulfide bonds arranged in a 
      conserved pattern. To date, studies of human defensins indicate that these 
      proteins are involved in various biological processes associated primarily with 
      defensive and regulatory responses to infections by pathological agents. A 
      comprehensive understanding of the multiple roles played by defensins within the 
      immune system is greatly increased by reviewing the results of detailed 
      structural studies. Emerging structural data, derived by the X-ray 
      crystallography and the NMR spectroscopy in solution combined with functional 
      studies; allow a rational understanding of the different activities of defensins 
      and the mechanisms controlling these activities. Due to their well-established 
      antimicrobial properties, defensins are also being investigated for their 
      potential as therapeutics agents. Recently, increased effort has been focused on 
      studies of the immunoregulatory properties of defensins, associated with their 
      ability to bind and activate the G(i)-protein-coupled seven-transmembrane 
      receptors. Comprehensive studies of defensins require development of simple, 
      efficient, and inexpensive methods to generate these proteins and their 
      derivatives in correctly folded form. This review highlights the current status 
      of the sample generation methods, structural studies, and the structure-function 
      relationships for human defensins.
FAU - Pazgier, Marzena
AU  - Pazgier M
AD  - Macromolecular Crystallography Laboratory, National Cancer Institute at 
      Frederick, Frederick, MD 21702, USA.
FAU - Li, Xiangqun
AU  - Li X
FAU - Lu, Wuyuan
AU  - Lu W
FAU - Lubkowski, Jacek
AU  - Lubkowski J
LA  - eng
PT  - Journal Article
PT  - Review
PL  - United Arab Emirates
TA  - Curr Pharm Des
JT  - Current pharmaceutical design
JID - 9602487
RN  - 0 (Anti-Infective Agents)
RN  - 0 (Defensins)
RN  - 0 (Receptors, G-Protein-Coupled)
RN  - 0 (Recombinant Proteins)
SB  - IM
MH  - Amino Acid Sequence
MH  - Anti-Infective Agents/*chemistry/classification/pharmacology
MH  - Crystallography, X-Ray
MH  - Defensins/*chemistry/classification/physiology
MH  - Humans
MH  - Immunity, Innate
MH  - Magnetic Resonance Spectroscopy
MH  - Molecular Sequence Data
MH  - Protein Structure, Tertiary
MH  - Receptors, G-Protein-Coupled/agonists
MH  - Recombinant Proteins/biosynthesis/chemical synthesis/chemistry
MH  - Structure-Activity Relationship
RF  - 282
EDAT- 2007/11/06 09:00
MHDA- 2008/03/22 09:00
CRDT- 2007/11/06 09:00
PHST- 2007/11/06 09:00 [pubmed]
PHST- 2008/03/22 09:00 [medline]
PHST- 2007/11/06 09:00 [entrez]
AID - 10.2174/138161207782110381 [doi]
PST - ppublish
SO  - Curr Pharm Des. 2007;13(30):3096-118. doi: 10.2174/138161207782110381.