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1hlm
From Proteopedia
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'''AMINO ACID SEQUENCE OF A GLOBIN FROM THE SEA CUCUMBER CAUDINA (MOLPADIA) ARENICOLA''' | '''AMINO ACID SEQUENCE OF A GLOBIN FROM THE SEA CUCUMBER CAUDINA (MOLPADIA) ARENICOLA''' | ||
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[[Category: Hackert, M L.]] | [[Category: Hackert, M L.]] | ||
[[Category: Mitchell, D T.]] | [[Category: Mitchell, D T.]] | ||
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Revision as of 15:59, 2 May 2008
AMINO ACID SEQUENCE OF A GLOBIN FROM THE SEA CUCUMBER CAUDINA (MOLPADIA) ARENICOLA
Overview
Coelomic cells from the sea cucumber Caudina (Molpadia) arenicola contain four major globins, A, B, C and D. The hemoglobins from this organism show unusual ligand-linked dissociation properties. The complete amino acid sequence of the D globin has been established. It is N-acetylated, consists of 158 residues and has a 10 amino acid N-terminal extension similar to that found in some other invertebrate globins. The C. arenicola D globin has an equal sequence identity (28%) with both alpha and beta human globins and as anticipated, is more closely related to these vertebrate proteins than are molluscan globins. The C. arenicola D globin shows a 59% identity with the globin I from the sea cucumber Paracaudina chilensis. The availability of the C. arenicola D globin sequence will aid the X-ray analysis of this protein and facilitate an understanding of the changes in subunit interactions that occur with cooperative ligand binding.
About this Structure
1HLM is a Single protein structure of sequence from Caudina arenicola. Full crystallographic information is available from OCA.
Reference
Amino acid sequence of a globin from the sea cucumber Caudina (Molpadia) arenicola., Mauri F, Omnaas J, Davidson L, Whitfill C, Kitto GB, Biochim Biophys Acta. 1991 May 30;1078(1):63-7. PMID:2049384 Page seeded by OCA on Fri May 2 18:59:08 2008
