PMID- 7540906
OWN - NLM
STAT- MEDLINE
DCOM- 19950803
LR  - 20181113
IS  - 0961-8368 (Print)
IS  - 1469-896X (Electronic)
IS  - 0961-8368 (Linking)
VI  - 4
IP  - 3
DP  - 1995 Mar
TI  - Comparative modeling of the three-dimensional structure of type II antifreeze 
      protein.
PG  - 460-71
AB  - Type II antifreeze proteins (AFP), which inhibit the growth of seed ice crystals 
      in the blood of certain fishes (sea raven, herring, and smelt), are the largest 
      known fish AFPs and the only class for which detailed structural information is 
      not yet available. However, a sequence homology has been recognized between these 
      proteins and the carbohydrate recognition domain of C-type lectins. The structure 
      of this domain from rat mannose-binding protein (MBP-A) has been solved by X-ray 
      crystallography (Weis WI, Drickamer K, Hendrickson WA, 1992, Nature 360:127-134) 
      and provided the coordinates for constructing the three-dimensional model of the 
      129-amino acid Type II AFP from sea raven, to which it shows 19% sequence 
      identity. Multiple sequence alignments between Type II AFPs, pancreatic stone 
      protein, MBP-A, and as many as 50 carbohydrate-recognition domain sequences from 
      various lectins were performed to determine reliably aligned sequence regions. 
      Successive molecular dynamics and energy minimization calculations were used to 
      relax bond lengths and angles and to identify flexible regions. The derived 
      structure contains two alpha-helices, two beta-sheets, and a high proportion of 
      amino acids in loops and turns. The model is in good agreement with preliminary 
      NMR spectroscopic analyses. It explains the observed differences in calcium 
      binding between sea raven Type II AFP and MBP-A. Furthermore, the model proposes 
      the formation of five disulfide bridges between Cys 7 and Cys 18, Cys 35 and Cys 
      125, Cys 69 and Cys 100, Cys 89 and Cys 111, and Cys 101 and Cys 117.(ABSTRACT 
      TRUNCATED AT 250 WORDS)
FAU - Sonnichsen, F D
AU  - Sonnichsen FD
AD  - Protein Engineering Network of Centres of Excellence, Edmonton, Canada.
FAU - Sykes, B D
AU  - Sykes BD
FAU - Davies, P L
AU  - Davies PL
LA  - eng
PT  - Comparative Study
PT  - Journal Article
PT  - Research Support, Non-U.S. Gov't
PL  - United States
TA  - Protein Sci
JT  - Protein science : a publication of the Protein Society
JID - 9211750
RN  - 0 (Antifreeze Proteins)
RN  - 0 (Calcium-Binding Proteins)
RN  - 0 (Carrier Proteins)
RN  - 0 (Cell Adhesion Molecules)
RN  - 0 (Disulfides)
RN  - 0 (E-Selectin)
RN  - 0 (Glycoproteins)
RN  - 0 (Lithostathine)
RN  - 0 (Mannose-Binding Lectin)
RN  - 0 (Nerve Tissue Proteins)
RN  - 143107-68-0 (mannose binding protein A)
SB  - IM
MH  - Adaptation, Physiological
MH  - Amino Acid Sequence
MH  - Animals
MH  - Antifreeze Proteins
MH  - Calcium-Binding Proteins/chemistry
MH  - Carrier Proteins/chemistry
MH  - Cell Adhesion Molecules/chemistry
MH  - Computer Simulation
MH  - Conserved Sequence
MH  - Crystallography, X-Ray
MH  - Disulfides/chemistry
MH  - E-Selectin
MH  - *Fishes
MH  - *Freezing
MH  - Glycoproteins/*chemistry
MH  - Lithostathine
MH  - Magnetic Resonance Spectroscopy
MH  - *Mannose-Binding Lectin
MH  - Models, Molecular
MH  - Molecular Sequence Data
MH  - *Nerve Tissue Proteins
MH  - Sequence Alignment
MH  - Sequence Homology, Amino Acid
MH  - Structure-Activity Relationship
PMC - PMC2143085
EDAT- 1995/03/01 00:00
MHDA- 1995/03/01 00:01
PMCR- 1995/09/01
CRDT- 1995/03/01 00:00
PHST- 1995/03/01 00:00 [pubmed]
PHST- 1995/03/01 00:01 [medline]
PHST- 1995/03/01 00:00 [entrez]
PHST- 1995/09/01 00:00 [pmc-release]
AID - 10.1002/pro.5560040313 [doi]
PST - ppublish
SO  - Protein Sci. 1995 Mar;4(3):460-71. doi: 10.1002/pro.5560040313.